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Conserved domains on  [gi|1907177247|ref|XP_036008548|]
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eukaryotic elongation factor 2 kinase isoform X4 [Mus musculus]

Protein Classification

Alpha_kinase_eEF2K and TPR domain-containing protein( domain architecture ID 13015117)

Alpha_kinase_eEF2K and TPR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
 1-176 4.34e-137

Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


:

Pssm-ID: 341217  Cd Length: 216  Bit Score: 397.09  E-value: 4.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPG 80
Cdd:cd16967    41 MRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYFEDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  81 QPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGV 160
Cdd:cd16967   121 SPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGL 200

                         170
                  ....*....|....*.
gi 1907177247 161 RGMALFFYSHACNRIC 176
Cdd:cd16967   201 RGMALFFHSHRCNPIC 216
TPR COG0790
TPR repeat [General function prediction only];
390-553 2.75e-12

TPR repeat [General function prediction only];


:

Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.88  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 390 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 469
Cdd:COG0790   107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 470 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 549
Cdd:COG0790   173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232


                  ....
gi 1907177247 550 LYTQ 553
Cdd:COG0790   233 WLRK 236
 
Name Accession Description Interval E-value
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
 1-176 4.34e-137

Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341217  Cd Length: 216  Bit Score: 397.09  E-value: 4.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPG 80
Cdd:cd16967    41 MRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYFEDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  81 QPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGV 160
Cdd:cd16967   121 SPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGL 200

                         170
                  ....*....|....*.
gi 1907177247 161 RGMALFFYSHACNRIC 176
Cdd:cd16967   201 RGMALFFHSHRCNPIC 216
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1-176 8.20e-89

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 272.69  E-value: 8.20e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247    1 MRECFRTKKLSNFLHaqQWKGASNYVAKRYIEPVdRSVYFEDVQLQMEAKLWGEDYNRHKP-PKQVDIMQMCIIELKDRP 79
Cdd:smart00811  24 MRVAFRVKDLSEDGS--GTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFNQLKPsPKKIEFLPSYVLELPDRS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   80 GQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLT-PQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNL 158
Cdd:smart00811 101 IPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEaPQAFSHFTYERSGGSLLVVDLQGVGDLLTDPQIHTEDGFGFGPGNL 180

                          170
                   ....*....|....*...
gi 1907177247  159 GVRGMALFFYSHACNRIC 176
Cdd:smart00811 181 GEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1-176 8.05e-72

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 228.37  E-value: 8.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSnflhaqQWKGASNYVAKRYIEPV---DRSVYFEDVQLQMEAKLWGEDYN------RHKPPKQVDIMQMC 71
Cdd:pfam02816   5 MRKAFKAKVDP------GDESGQNYVAKEFKKIVygvELEYYFEDAQSQALAKELAEEFNaearalENFPPKKIEFIPPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  72 IIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDN--IRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEK 149
Cdd:pfam02816  79 VVELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEDdeLEQTMQAFSHFTYERSGGQLLVCDLQGVGNLLTDPAIHTKD 158

                         170       180
                  ....*....|....*....|....*..
gi 1907177247 150 GTDFGDGNLGVRGMALFFYSHACNRIC 176
Cdd:pfam02816 159 GKRFGDTNLGEEGIASFFSTHKCNKIC 185
TPR COG0790
TPR repeat [General function prediction only];
390-553 2.75e-12

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.88  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 390 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 469
Cdd:COG0790   107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 470 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 549
Cdd:COG0790   173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232


                  ....
gi 1907177247 550 LYTQ 553
Cdd:COG0790   233 WLRK 236
 
Name Accession Description Interval E-value
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
 1-176 4.34e-137

Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341217  Cd Length: 216  Bit Score: 397.09  E-value: 4.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPG 80
Cdd:cd16967    41 MRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYFEDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  81 QPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGV 160
Cdd:cd16967   121 SPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGL 200

                         170
                  ....*....|....*.
gi 1907177247 161 RGMALFFYSHACNRIC 176
Cdd:cd16967   201 RGMALFFHSHRCNPIC 216
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1-176 8.20e-89

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 272.69  E-value: 8.20e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247    1 MRECFRTKKLSNFLHaqQWKGASNYVAKRYIEPVdRSVYFEDVQLQMEAKLWGEDYNRHKP-PKQVDIMQMCIIELKDRP 79
Cdd:smart00811  24 MRVAFRVKDLSEDGS--GTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFNQLKPsPKKIEFLPSYVLELPDRS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   80 GQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLT-PQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNL 158
Cdd:smart00811 101 IPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEaPQAFSHFTYERSGGSLLVVDLQGVGDLLTDPQIHTEDGFGFGPGNL 180

                          170
                   ....*....|....*...
gi 1907177247  159 GVRGMALFFYSHACNRIC 176
Cdd:smart00811 181 GEEGIEKFFATHKCNSIC 198
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
 1-176 5.57e-84

Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed of alpha-kinase domains of Dictyostelium discoideum myosin heavy chain kinases A-D (MHCKA, MHCKB, MHCKC, MHCKD), alpha-protein kinase 1 (AK1), and similar proteins. The myosin heavy chain kinases are involved in regulating myosin II filament assembly in Dictyostelium discoideum. They phosphorylate target threonine residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail, resulting in filament disassembly. The different MHCK isoforms display different spatial regulation, indicating specific roles for each isoform in fine tuning the Dictyostelium actomyosin cytoskeleton. They all contain an alpha-kinase domain as well as WD40 repeats at the C-terminus. AK1 contains an N-terminal Arf-GAP domain and a central alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341218  Cd Length: 202  Bit Score: 260.63  E-value: 5.57e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSNFlhaqqwKGASNYVAKRYIEP-VDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRP 79
Cdd:cd16968    33 LREAYHLKDLSAP------GPSTLFVAKLSKDPnESRETYFEDVEMQMVCKKWAEKFNAKNPPKKVEFLPAWVLELVDRP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  80 GQPLFHLEHYIEGKYIKYNSNSGFVRDDNiRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLG 159
Cdd:cd16968   107 PPPLCGVEPFIEGEYVKHNNNFGYVDEDE-RNTPQAFSHFTYEASGHQLLVVDIQGVGDLYTDPQIHTIDGKGFGKGNLG 185

                         170
                  ....*....|....*..
gi 1907177247 160 VRGMALFFYSHACNRIC 176
Cdd:cd16968   186 QKGIEKFLETHKCNAIC 202
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1-176 8.05e-72

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 228.37  E-value: 8.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSnflhaqQWKGASNYVAKRYIEPV---DRSVYFEDVQLQMEAKLWGEDYN------RHKPPKQVDIMQMC 71
Cdd:pfam02816   5 MRKAFKAKVDP------GDESGQNYVAKEFKKIVygvELEYYFEDAQSQALAKELAEEFNaearalENFPPKKIEFIPPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  72 IIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDN--IRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEK 149
Cdd:pfam02816  79 VVELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEDdeLEQTMQAFSHFTYERSGGQLLVCDLQGVGNLLTDPAIHTKD 158

                         170       180
                  ....*....|....*....|....*..
gi 1907177247 150 GTDFGDGNLGVRGMALFFYSHACNRIC 176
Cdd:pfam02816 159 GKRFGDTNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
 1-176 1.62e-63

Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341214  Cd Length: 213  Bit Score: 207.64  E-value: 1.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247   1 MRECFRTKKLSNFlhaqqwkgASNYVAKRYIEPVDRSV----YFEDVQLQMEAKLWGEDYNRHK-----PPKQVDIMQMC 71
Cdd:cd04515    35 MREAFKAKDLDSK--------GKKYVAKRFKRIGDPEEnledLFDELRMQALAQYLAKEFNARAksknlIAPKINFVDPF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  72 IIELKDR--PGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEK 149
Cdd:cd04515   107 VVKLGDRddPGKVVFLVEPFLEGKFVKYNNNNGMVNDEDLGETAQAFSHFTYERSGGQLLVTDLQGVGLVLTDPQIHTVD 186

                         170       180
                  ....*....|....*....|....*..
gi 1907177247 150 GTDFGDGNLGVRGMALFFYSHACNRIC 176
Cdd:cd04515   187 GGGFGLGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
 26-176 7.23e-34

Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium discoideum alpha-protein kinase VwkA is also called von Willebrand factor A alpha-kinase or vWF kinase. It influences myosin II abundance and assembly behavior as vWKA gene disruption leads to significant myosin II overassembly. VwkA also serves a critical conserved role in the periodic contractions of the contractile vacuole through its regulation of the myosin II cortical cytoskeleton. It contains a vWFa domain (named after its homology to von Willebrand factor A, a plasma glycoprotein essential for proper blood clotting) and a C-terminal alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341220  Cd Length: 227  Bit Score: 128.61  E-value: 7.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  26 VAKRYIEPVDRSV-----YFEDVQLQ-MEAKLwGEDYN----RHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYI 95
Cdd:cd16970    64 VLKEFKTPGSAQRnsrerYLESMEVQtVAAKL-AFEFNkllaRAGINKKITFLEAKVLRVANGDSPQYYTMESFLEGEYK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  96 KYNSNSGFVRDDNiRLTPQAFSHFTFERSGHQLIVVDIQGV-----GDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSH 170
Cdd:cd16970   143 KFNNNVGVVNEDE-VEILQAFSHWTYEASKGYLMVVDLQGVrtdddGFLLTDPAIHCTDVLRFGRTNLGKEGIDKFFATH 221


                  ....*.
gi 1907177247 171 ACNRIC 176
Cdd:cd16970   222 KCNQHC 227
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 46-176 3.77e-28

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341225  Cd Length: 243  Bit Score: 112.86  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  46 QMEAKLWGEDYNR------HKPPKQVDIMQMCIIELKD--RPGQPLFHLEHYIEGKYIKYNSNSGFVR------------ 105
Cdd:cd17508    81 QSTAQELAERFNKrlralpGGPAPRVKFLPCHVYKTKDvsYRGRAWVLVEKELEGKFTKWNTNAGGVKksiesvgegrge 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 106 DDNIRLT----PQAFSHFTFERSGHQLIVVDIQGV------GDLYTDPQIHTEKGT--DFGDGNLGVRGMALFFYSHACN 173
Cdd:cd17508   161 SNSSRLRvddvPQAFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHVSGKrhRFGATDKGLEGIRNFLRTHKCS 240


                  ...
gi 1907177247 174 RIC 176
Cdd:cd17508   241 PLC 243
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
 13-176 4.35e-24

Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called chromosome 4 kinase or lymphocyte alpha-protein kinase (LAK). ALPK1 is implicated in epithelial cell polarity and exocytic vesicular transport towards the apical plasma membrane. It resides on Golgi-derived vesicles where it phosphorylates myosin IA, a motor protein that regulates the delivery of vesicles to the plasma-membrane. It may be associated with inflammation-related diseases such as gout and type 2 diabetes mellitus. ALPK1 contains a C-terminal alpha-kinase domain, an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341219  Cd Length: 227  Bit Score: 101.01  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  13 FLHaqQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNR----HKPPKQVDIMQMCIIE-LKDRPGQPLFHLE 87
Cdd:cd16969    51 FLH--QEETLGRYVGKEYKKPKELQYHFNDVERQMTAQHYVTEFNKrlyeQNIPTQIFFIPSVILLiLEDKGIKGCVSVE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  88 HYIEGKYIKYNSNSGFVRDDNiRLTPQ--AFSHFTFERSGHQLIVVDIQG------VGDLY-TDPQIHTEKGTdFGDGNL 158
Cdd:cd16969   129 PYMLGEFVKLTNNTTVKKEEY-KATDYglAYGHFTYEFSNHQDVVVDLQGwvtangKGLTYlTDPQIHSVVKK-SGTTNF 206

                         170       180
                  ....*....|....*....|
gi 1907177247 159 GVRGMALFFYSH--ACNRIC 176
Cdd:cd16969   207 GKKGIEYFFNNQhtECNEIC 226
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 87-176 3.09e-16

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341226  Cd Length: 221  Bit Score: 77.77  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  87 EHYIEGkYIKYNSNSG-FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGD----LYTDPQIHTEKGTDFGDGNLGVR 161
Cdd:cd17509   128 EPFIEN-YEKFNSNSGwNDDSKGWGEVMQALSHFSYHISGGKYLLCDLQGGVYkneyVLTDPVILSRTGREYGVTDLGPE 206

                          90
                  ....*....|....*
gi 1907177247 162 GMALFFYSHACNRIC 176
Cdd:cd17509   207 GIWNFFANHKCNKYC 221
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
 86-177 5.99e-15

Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6; Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341222  Cd Length: 239  Bit Score: 74.65  E-value: 5.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  86 LEHYIEGKYIKYNSNSGfvrdDNIrlTPQ--------AFSHFTFERSGHQLIVVDIQGVGDLYTDPQI-----HTEKGTD 152
Cdd:cd16972   140 IEKYLTGEFRKYNNNNG----DEI--TPTslleetllAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikpedKQSRGMV 213

                          90       100
                  ....*....|....*....|....*
gi 1907177247 153 FGDGNLGVRGMALFFYSHACNRICQ 177
Cdd:cd16972   214 FGPANLGEDAIRNFIAKHHCNSCCR 238
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
 20-177 1.05e-13

Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) and 2 (ChaK2), and similar proteins. ChaK1 and ChaK2 are also called transient receptor potential cation channel subfamily M members 7 (TRMP7) and 6 (TRMP6), respectively. They are fusion proteins containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. They are both cation-selective channels that preferentially permeate Zn2+, Mg2+, and Ca2+ ions. They are central regulators of Mg2+ and Ca2+ homeostasis. TRMP7 is ubiquitously expressed while TRMP6 is highly expressed in specific tissues such as the kidney and intestine. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341215  Cd Length: 239  Bit Score: 71.14  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  20 KGASNYVAKRYIEPVDR---SVYFED---------VQLQMEAKLWGEDYNRHKP---PKQVDIMQMCIIELKDrPGQpLF 84
Cdd:cd16965    61 KLGSVYIVKSFLPEVVRtwqKIFPEStvlhlclreIQQQRAAQKLMQRFNQVKPssiPYSPRFLEVFLLYCHS-AGQ-WL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  85 HLEHYIEGKYIKYNSNSG--FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI-----HTEKGTDFGDGN 157
Cdd:cd16965   139 TVENNMTGEFRKYNNNNGdeILPTNTLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikvedKSSGEMVFGPAN 218

                         170       180
                  ....*....|....*....|
gi 1907177247 158 LGVRGMALFFYSHACNRICQ 177
Cdd:cd16965   219 LGEDAIQNFVAKHHCNSCCR 238
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
 84-177 1.41e-13

Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation channel subfamily M member 7; Channel kinase 1 (ChaK1), also called transient receptor potential cation channel subfamily M member 7 (TRMP7) or long transient receptor potential channel 7 (LTrpC7), is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is ubiquitously expressed and is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM7 plays a role in cancer proliferation, stroke, hydrogen peroxide dependent neurodegeneration, and heavy metal toxicity. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341221  Cd Length: 239  Bit Score: 70.80  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  84 FHLEHYIEGKYIKYNSNSG--FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI--HTEKGTD---FGDG 156
Cdd:cd16971   138 FAVEECMTGEFRKYNNNNGdeIIPTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikAGEKRSYdmvFGPA 217

                          90       100
                  ....*....|....*....|.
gi 1907177247 157 NLGVRGMALFFYSHACNRICQ 177
Cdd:cd16971   218 NLGEDAIKNFRAKHHCNSCCR 238
TPR COG0790
TPR repeat [General function prediction only];
390-553 2.75e-12

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.88  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 390 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 469
Cdd:COG0790   107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 470 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 549
Cdd:COG0790   173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232


                  ....
gi 1907177247 550 LYTQ 553
Cdd:COG0790   233 WLRK 236
TPR COG0790
TPR repeat [General function prediction only];
405-553 4.47e-11

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 63.41  E-value: 4.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 405 DRESAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNL 484
Cdd:COG0790    82 DYEKALEWFEKAAEQGDAEAQYNLGLMYEE----------GLGVPQDYAKALEWYEKAAEQGDADAQYNLGLLYLNGEGV 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907177247 485 SpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGDLYTQ 553
Cdd:COG0790   152 P----KDPAKAAEWYRKAA------EQGDADA-----QYNL----GVLYEN-GRGVPKDPAKALEWYRK 200
TPR COG0790
TPR repeat [General function prediction only];
390-504 2.66e-10

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 61.10  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 390 RYHEGGRFCEKDEEWdresAIFHLEHAADLGELEAIVGLGLMYSQLphhiladvslKETEENKTKGFDYLLKAAEAGDRH 469
Cdd:COG0790   143 LLYLNGEGVPKDPAK----AAEWYRKAAEQGDADAQYNLGVLYENG----------RGVPKDPAKALEWYRKAAEQGDAD 208

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907177247 470 SMILVARAFDTGLNLSPDRcqdwSEALHWYNTALE 504
Cdd:COG0790   209 AQYNLGRLYLNGEGVEKDL----EKALRWLRKAAE 239
TPR COG0790
TPR repeat [General function prediction only];
413-553 2.07e-07

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 52.24  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247 413 LEHAADLGELEAIVGLGLMYSQLphhiladvslKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNLSpdrcQDW 492
Cdd:COG0790    54 AAAAAAAGGAEAQYNLGLMYAEG----------RGVPKDYEKALEWFEKAAEQGDAEAQYNLGLMYEEGLGVP----QDY 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907177247 493 SEALHWYNTALEttdcdeggeydgiQDEP--QYALlareAEMLLTgGFGLDKNPQRSGDLYTQ 553
Cdd:COG0790   120 AKALEWYEKAAE-------------QGDAdaQYNL----GLLYLN-GEGVPKDPAKAAEWYRK 164
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
 41-176 3.06e-05

Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341224  Cd Length: 239  Bit Score: 45.58  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  41 EDVQLQMEAKLWGEDYNRHKPPKQV--DIMQMCIIELKDRPGQ--PLFHLEHYIEGKYIKYNSNSG-----FVRDDNIRL 111
Cdd:cd16974    94 QECYVQNTAREYAKIYAAEAQPLEGfgEVPEIIPIFLIHRPANniPYATVEEELIGDFVKYSVRDGkeinvLRRDSEAGQ 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907177247 112 TPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHT-EKGTDFGDGNLGVRGMALFFYSHACNRIC 176
Cdd:cd16974   174 KCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATcSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
 73-176 1.16e-04

Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 (ALPK3) are also called heart alpha-protein kinase (HAK) and muscle alpha-protein kinase (MAK), respectively. They both contain a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341216  Cd Length: 239  Bit Score: 44.10  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177247  73 IELKDRPGQ--PLFHLEHYIEGKYIKYNSNSG-----FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI 145
Cdd:cd16966   128 LFLIYRPANniPYATVEEELIGPFVKYSIRDGkeinfLRSESEAGQKCCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGI 207

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907177247 146 HTE-KGTDFGDGNLGVRGMALFFYSHACNRIC 176
Cdd:cd16966   208 ATLaKGYQGLKGNCSMTFIDQFAALHQCNKYC 239
 
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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