NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6681275|ref|NP_031934|]
View 

eukaryotic elongation factor 2 kinase isoform a [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
102-317 2.51e-163

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: 469.12  E-value: 2.51e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  102 HLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYF 181
Cdd:cd16967   1 HLEDLPTERAVRHRYNAATKKWTKDEVLVKMESKPFARGAMRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  182 EDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFT 261
Cdd:cd16967  81 EDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPGSPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681275  262 FERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16967 161 FERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGLRGMALFFHSHRCNPIC 216
TPR COG0790
TPR repeat [General function prediction only];
531-694 5.18e-12

TPR repeat [General function prediction only];


:

Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.49  E-value: 5.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  531 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 610
Cdd:COG0790 107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  611 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 690
Cdd:COG0790 173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232

                ....
gi 6681275  691 LYTQ 694
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 ...
102-317 2.51e-163

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: 469.12  E-value: 2.51e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  102 HLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYF 181
Cdd:cd16967   1 HLEDLPTERAVRHRYNAATKKWTKDEVLVKMESKPFARGAMRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  182 EDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFT 261
Cdd:cd16967  81 EDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPGSPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681275  262 FERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16967 161 FERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGLRGMALFFHSHRCNPIC 216
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
120-317 3.91e-97

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: 298.50  E-value: 3.91e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275     120 TGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHaqQWKGASNYVAKRYIEPVdRSVYFEDVQLQMEAKLWGEDYNR 199
Cdd:smart00811   2 SGKWTVSETGVKIELKPFAKGAMRVAFRVKDLSEDGS--GTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFNQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275     200 HKP-PKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLT-PQAFSHFTFERSGHQLIVVDIQGV 277
Cdd:smart00811  79 LKPsPKKIEFLPSYVLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEaPQAFSHFTYERSGGSLLVVDLQGV 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 6681275     278 GDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:smart00811 159 GDLLTDPQIHTEDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
138-317 1.99e-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: 232.99  E-value: 1.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275    138 GRGAMRECFRTKKLSnflhaqQWKGASNYVAKRYIEPV---DRSVYFEDVQLQMEAKLWGEDYN------RHKPPKQVDI 208
Cdd:pfam02816   1 AEGAMRKAFKAKVDP------GDESGQNYVAKEFKKIVygvELEYYFEDAQSQALAKELAEEFNaearalENFPPKKIEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275    209 MQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDN--IRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI 286
Cdd:pfam02816  75 IPPYVVELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEDdeLEQTMQAFSHFTYERSGGQLLVCDLQGVGNLLTDPAI 154
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6681275    287 HTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:pfam02816 155 HTKDGKRFGDTNLGEEGIASFFSTHKCNKIC 185
TPR COG0790
TPR repeat [General function prediction only];
531-694 5.18e-12

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.49  E-value: 5.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  531 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 610
Cdd:COG0790 107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  611 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 690
Cdd:COG0790 173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232

                ....
gi 6681275  691 LYTQ 694
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 ...
102-317 2.51e-163

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: 469.12  E-value: 2.51e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  102 HLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYF 181
Cdd:cd16967   1 HLEDLPTERAVRHRYNAATKKWTKDEVLVKMESKPFARGAMRECYRAKKLSNFSHNQDWKHASNYVAKRYIEPVDREVYF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  182 EDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFT 261
Cdd:cd16967  81 EDVRLQMDAKLWGEEYNRHNPPKKVDIMQMCVLEFVDRPGSPLYHLEHFIEGDYIKYNSNSGFVRDDDIRLTPQAFSHFT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681275  262 FERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16967 161 FERSGHQLIVVDIQGVGDLYTDPQIHTADGEGYGDGNLGLRGMALFFHSHRCNPIC 216
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
120-317 3.91e-97

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: 298.50  E-value: 3.91e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275     120 TGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHaqQWKGASNYVAKRYIEPVdRSVYFEDVQLQMEAKLWGEDYNR 199
Cdd:smart00811   2 SGKWTVSETGVKIELKPFAKGAMRVAFRVKDLSEDGS--GTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFNQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275     200 HKP-PKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLT-PQAFSHFTFERSGHQLIVVDIQGV 277
Cdd:smart00811  79 LKPsPKKIEFLPSYVLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEaPQAFSHFTYERSGGSLLVVDLQGV 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 6681275     278 GDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:smart00811 159 GDLLTDPQIHTEDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
111-317 2.16e-95

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: 293.75  E-value: 2.16e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  111 ATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFlhaqqwKGASNYVAKRYIEP-VDRSVYFEDVQLQME 189
Cdd:cd16968   2 AIKHEFDPETGKWTSTATKVKIDPKPFAEGALREAYHLKDLSAP------GPSTLFVAKLSKDPnESRETYFEDVEMQMV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  190 AKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNiRLTPQAFSHFTFERSGHQL 269
Cdd:cd16968  76 CKKWAEKFNAKNPPKKVEFLPAWVLELVDRPPPPLCGVEPFIEGEYVKHNNNFGYVDEDE-RNTPQAFSHFTYEASGHQL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6681275  270 IVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16968 155 LVVDIQGVGDLYTDPQIHTIDGKGFGKGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
138-317 1.99e-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: 232.99  E-value: 1.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275    138 GRGAMRECFRTKKLSnflhaqQWKGASNYVAKRYIEPV---DRSVYFEDVQLQMEAKLWGEDYN------RHKPPKQVDI 208
Cdd:pfam02816   1 AEGAMRKAFKAKVDP------GDESGQNYVAKEFKKIVygvELEYYFEDAQSQALAKELAEEFNaearalENFPPKKIEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275    209 MQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDN--IRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI 286
Cdd:pfam02816  75 IPPYVVELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEDdeLEQTMQAFSHFTYERSGGQLLVCDLQGVGNLLTDPAI 154
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6681275    287 HTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:pfam02816 155 HTKDGKRFGDTNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
109-317 6.36e-68

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: 222.27  E-value: 6.36e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  109 EHATRHRYNAVTGEWLKDEVLIKMASQ-PFGRGAMRECFRTKKLSNFlhaqqwkgASNYVAKRYIEPVDRSV----YFED 183
Cdd:cd04515   1 EIEVLRLISVTDLKWTTEETTVRVAKKkPFAQGAMREAFKAKDLDSK--------GKKYVAKRFKRIGDPEEnledLFDE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  184 VQLQMEAKLWGEDYNRHK-----PPKQVDIMQMCIIELKDR--PGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQA 256
Cdd:cd04515  73 LRMQALAQYLAKEFNARAksknlIAPKINFVDPFVVKLGDRddPGKVVFLVEPFLEGKFVKYNNNNGMVNDEDLGETAQA 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6681275  257 FSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd04515 153 FSHFTYERSGGQLLVTDLQGVGLVLTDPQIHTVDGGGFGLGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
122-317 5.26e-38

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: 141.32  E-value: 5.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  122 EWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHaqqwkgaSNYVAKRYIEPVDRSV-----YFEDVQLQ-MEAKLwGE 195
Cdd:cd16970  26 EMSIREITVKIAPPPFAKGAERWAYYALDTTSDST-------KKVVLKEFKTPGSAQRnsrerYLESMEVQtVAAKL-AF 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  196 DYN----RHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNiRLTPQAFSHFTFERSGHQLIV 271
Cdd:cd16970  98 EFNkllaRAGINKKITFLEAKVLRVANGDSPQYYTMESFLEGEYKKFNNNVGVVNEDE-VEILQAFSHWTYEASKGYLMV 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6681275  272 VDIQGV-----GDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16970 177 VDLQGVrtdddGFLLTDPAIHCTDVLRFGRTNLGKEGIDKFFATHKCNQHC 227
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
127-317 5.91e-31

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: 121.72  E-value: 5.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  127 EVLIKMASQPFGRGAMRECFRTKKLSN--FLHAQQWKGASnYVAK--RYIEPVDRSVYFEDVQL--QMEAKLWGEDYNR- 199
Cdd:cd17508  16 AFGIAVRKLPFGEGAERNVFRCTEISKegGTKTATKIGPR-LVAKesRHAEDESFDIKFHKKFCktQSTAQELAERFNKr 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  200 -----HKPPKQVDIMQMCIIELKD--RPGQPLFHLEHYIEGKYIKYNSNSGFVR------------DDNIRLT----PQA 256
Cdd:cd17508  95 lralpGGPAPRVKFLPCHVYKTKDvsYRGRAWVLVEKELEGKFTKWNTNAGGVKksiesvgegrgeSNSSRLRvddvPQA 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6681275  257 FSHFTFERSGHQLIVVDIQGV------GDLYTDPQIHTEKGT--DFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd17508 175 FSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHVSGKrhRFGATDKGLEGIRNFLRTHKCSPLC 243
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
115-317 1.83e-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: 102.55  E-value: 1.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  115 RYNAVTGEWLKDEVLI------KMASQpfgrGAMRECFRTKklsnFLHaqQWKGASNYVAKRYIEPVDRSVYFEDVQLQM 188
Cdd:cd16969  14 KYSKKSGLWTAQETMVyigdnlQVGKQ----GKQRNAFWVH----FLH--QEETLGRYVGKEYKKPKELQYHFNDVERQM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  189 EAKLWGEDYNR----HKPPKQVDIMQMCIIE-LKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNiRLTPQ--AFSHFT 261
Cdd:cd16969  84 TAQHYVTEFNKrlyeQNIPTQIFFIPSVILLiLEDKGIKGCVSVEPYMLGEFVKLTNNTTVKKEEY-KATDYglAYGHFT 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681275  262 FERSGHQLIVVDIQG------VGDLY-TDPQIHTEKGTdFGDGNLGVRGMALFFYSH--ACNRIC 317
Cdd:cd16969 163 YEFSNHQDVVVDLQGwvtangKGLTYlTDPQIHSVVKK-SGTTNFGKKGIEYFFNNQhtECNEIC 226
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
228-317 5.60e-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: 77.39  E-value: 5.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  228 EHYIEGkYIKYNSNSG-FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGD----LYTDPQIHTEKGTDFGDGNLGVR 302
Cdd:cd17509 128 EPFIEN-YEKFNSNSGwNDDSKGWGEVMQALSHFSYHISGGKYLLCDLQGGVYkneyVLTDPVILSRTGREYGVTDLGPE 206
                        90
                ....*....|....*
gi 6681275  303 GMALFFYSHACNRIC 317
Cdd:cd17509 207 GIWNFFANHKCNKYC 221
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
227-318 7.99e-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: 7.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  227 LEHYIEGKYIKYNSNSGfvrdDNIrlTPQ--------AFSHFTFERSGHQLIVVDIQGVGDLYTDPQI-----HTEKGTD 293
Cdd:cd16972 140 IEKYLTGEFRKYNNNNG----DEI--TPTslleetllAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikpedKQSRGMV 213
                        90       100
                ....*....|....*....|....*
gi 6681275  294 FGDGNLGVRGMALFFYSHACNRICQ 318
Cdd:cd16972 214 FGPANLGEDAIRNFIAKHHCNSCCR 238
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
135-318 5.98e-14

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: 71.91  E-value: 5.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  135 QPFGRGAMRECFR--TKKLSNFLHAQQWKGASNYVAKRYIEPVDR---SVYFED---------VQLQMEAKLWGEDYNRH 200
Cdd:cd16965  33 QPLSQEEMDGGLRraTKVVCTWSEGDILKLGSVYIVKSFLPEVVRtwqKIFPEStvlhlclreIQQQRAAQKLMQRFNQV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  201 KP---PKQVDIMQMCIIELKDrPGQpLFHLEHYIEGKYIKYNSNSG--FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQ 275
Cdd:cd16965 113 KPssiPYSPRFLEVFLLYCHS-AGQ-WLTVENNMTGEFRKYNNNNGdeILPTNTLEETMLAFSHWTYEYTRGELLVLDLQ 190
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6681275  276 GVGDLYTDPQI-----HTEKGTDFGDGNLGVRGMALFFYSHACNRICQ 318
Cdd:cd16965 191 GVGENLTDPSVikvedKSSGEMVFGPANLGEDAIQNFVAKHHCNSCCR 238
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
225-318 1.87e-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: 1.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  225 FHLEHYIEGKYIKYNSNSG--FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI--HTEKGTD---FGDG 297
Cdd:cd16971 138 FAVEECMTGEFRKYNNNNGdeIIPTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikAGEKRSYdmvFGPA 217
                        90       100
                ....*....|....*....|.
gi 6681275  298 NLGVRGMALFFYSHACNRICQ 318
Cdd:cd16971 218 NLGEDAIKNFRAKHHCNSCCR 238
TPR COG0790
TPR repeat [General function prediction only];
531-694 5.18e-12

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 66.49  E-value: 5.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  531 RYHEGGRFCEKDEEwdreSAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRH 610
Cdd:COG0790 107 LMYEEGLGVPQDYA----KALEWYEKAAEQGDADAQYNLGLLYLN----------GEGVPKDPAKAAEWYRKAAEQGDAD 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  611 SMILVARAFDTGLNLSpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGD 690
Cdd:COG0790 173 AQYNLGVLYENGRGVP----KDPAKALEWYRKAA------EQGDADA-----QYNL----GRLYLN-GEGVEKDLEKALR 232

                ....
gi 6681275  691 LYTQ 694
Cdd:COG0790 233 WLRK 236
TPR COG0790
TPR repeat [General function prediction only];
546-694 8.63e-11

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 62.64  E-value: 8.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  546 DRESAIFHLEHAADLGELEAIVGLGLMYSQlphhiladvsLKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNL 625
Cdd:COG0790  82 DYEKALEWFEKAAEQGDAEAQYNLGLMYEE----------GLGVPQDYAKALEWYEKAAEQGDADAQYNLGLLYLNGEGV 151
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6681275  626 SpdrcQDWSEALHWYNTALettdcdEGGEYDGiqdepQYALlareAEMLLTgGFGLDKNPQRSGDLYTQ 694
Cdd:COG0790 152 P----KDPAKAAEWYRKAA------EQGDADA-----QYNL----GVLYEN-GRGVPKDPAKALEWYRK 200
TPR COG0790
TPR repeat [General function prediction only];
531-645 4.66e-10

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 60.71  E-value: 4.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  531 RYHEGGRFCEKDEEWdresAIFHLEHAADLGELEAIVGLGLMYSQLphhiladvslKETEENKTKGFDYLLKAAEAGDRH 610
Cdd:COG0790 143 LLYLNGEGVPKDPAK----AAEWYRKAAEQGDADAQYNLGVLYENG----------RGVPKDPAKALEWYRKAAEQGDAD 208
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6681275  611 SMILVARAFDTGLNLSPDRcqdwSEALHWYNTALE 645
Cdd:COG0790 209 AQYNLGRLYLNGEGVEKDL----EKALRWLRKAAE 239
TPR COG0790
TPR repeat [General function prediction only];
554-694 3.54e-07

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 51.85  E-value: 3.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  554 LEHAADLGELEAIVGLGLMYSQLphhiladvslKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNLSpdrcQDW 633
Cdd:COG0790  54 AAAAAAAGGAEAQYNLGLMYAEG----------RGVPKDYEKALEWFEKAAEQGDAEAQYNLGLMYEEGLGVP----QDY 119
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6681275  634 SEALHWYNTALEttdcdeggeydgiQDEP--QYALlareAEMLLTgGFGLDKNPQRSGDLYTQ 694
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 ...
137-317 9.98e-07

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: 50.59  E-value: 9.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  137 FGRGAMRECFRTKKLSNFL------HAQQWK--GASNYVAKRYIEPVDRS--VYFEDVQLQMEAKLWGEDYNRHKPPKQV 206
Cdd:cd16974  39 FGEGMHRKAFRSKVMCGLLpvflpgHACVLKvhNAIAYGTKNNDELIQKNykLAVQECYVQNTAREYAKIYAAEAQPLEG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  207 --DIMQMCIIELKDRPGQ--PLFHLEHYIEGKYIKYNSNSG-----FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGV 277
Cdd:cd16974 119 fgEVPEIIPIFLIHRPANniPYATVEEELIGDFVKYSVRDGkeinvLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGV 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6681275  278 GDLYTDPQIHT-EKGTDFGDGNLGVRGMALFFYSHACNRIC 317
Cdd:cd16974 199 GMKLTDVGIATcSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
214-317 1.73e-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: 43.72  E-value: 1.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681275  214 IELKDRPGQ--PLFHLEHYIEGKYIKYNSNSG-----FVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQI 286
Cdd:cd16966 128 LFLIYRPANniPYATVEEELIGPFVKYSIRDGkeinfLRSESEAGQKCCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGI 207
                        90       100       110
                ....*....|....*....|....*....|..
gi 6681275  287 HTE-KGTDFGDGNLGVRGMALFFYSHACNRIC 317
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH