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Conserved domains on  [gi|254553408|ref|NP_082084|]
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alpha-protein kinase 1 [Mus musculus]

Protein Classification

Alpha_kinase_ALPK1 domain-containing protein( domain architecture ID 13015130)

Alpha_kinase_ALPK1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
 990-1216 1.13e-161

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: 480.43  E-value: 1.13e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  990 SNQLQQAHSALLLKYSKKSELWTAQETVVYLGDYLKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYKERKGLRHHFTDVE 1069
Cdd:cd16969     1 PDQLKRAHDALLLKYSKKSGLWTAQETMVYIGDNLQVGKQGKQRNAFWVHFLHQEETLGRYVGKEYKKPKELQYHFNDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1070 RQMTAQHYVTEFNKRLYEQKIPTQIFYIPSTILLILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYGLAYGH 1149
Cdd:cd16969    81 RQMTAQHYVTEFNKRLYEQNIPTQIFFIPSVILLILEDKGIKGCVSVEPYMLGEFVKLTNNTTVKKEEYKATDYGLAYGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553408 1150 FSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKDVTTNFGKRGIFYFFNNQHASCNEICH 1216
Cdd:cd16969   161 FTYEFSNHQDVVVDLQGWVTANGKGLTYLTDPQIHSVVKKSGTTNFGKKGIEYFFNNQHTECNEICR 227
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
 990-1216 1.13e-161

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: 480.43  E-value: 1.13e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  990 SNQLQQAHSALLLKYSKKSELWTAQETVVYLGDYLKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYKERKGLRHHFTDVE 1069
Cdd:cd16969     1 PDQLKRAHDALLLKYSKKSGLWTAQETMVYIGDNLQVGKQGKQRNAFWVHFLHQEETLGRYVGKEYKKPKELQYHFNDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1070 RQMTAQHYVTEFNKRLYEQKIPTQIFYIPSTILLILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYGLAYGH 1149
Cdd:cd16969    81 RQMTAQHYVTEFNKRLYEQNIPTQIFFIPSVILLILEDKGIKGCVSVEPYMLGEFVKLTNNTTVKKEEYKATDYGLAYGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553408 1150 FSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKDVTTNFGKRGIFYFFNNQHASCNEICH 1216
Cdd:cd16969   161 FTYEFSNHQDVVVDLQGWVTANGKGLTYLTDPQIHSVVKKSGTTNFGKKGIEYFFNNQHTECNEICR 227
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1007-1215 2.65e-63

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: 213.76  E-value: 2.65e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408   1007 KSELWTAQETVVYLgdYLKVKKKGKQRNAFWVHYL----HQEETLGRYVGKEYKERKgLRHHFTDVERQMTAQHYVTEFN 1082
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLsedgSGTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFN 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408   1083 KRlyeQKIPTQIFYIPSTILLILeDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYGLAYGHFSYEFSNHRDVVV 1162
Cdd:smart00811   78 QL---KPSPKKIEFLPSYVLELP-DRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEAPQAFSHFTYERSGGSLLVV 153

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 254553408   1163 DLQGWvtGNgkgliYLTDPQIHSVD-QKDVTTNFGKRGIFYFFNNQHasCNEIC 1215
Cdd:smart00811  154 DLQGV--GD-----LLTDPQIHTEDgFGFGPGNLGEEGIEKFFATHK--CNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1029-1215 1.18e-52

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: 182.53  E-value: 1.18e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  1029 KGKQRNAFWVHYLHQEETLGRYVGKEYKE---RKGLRHHFTDVERQMTAQHYVTEFNK--RLYEQKIPTQIFYIPSTILl 1103
Cdd:pfam02816    2 EGAMRKAFKAKVDPGDESGQNYVAKEFKKivyGVELEYYFEDAQSQALAKELAEEFNAeaRALENFPPKKIEFIPPYVV- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  1104 ILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNE-YKATEYGLAYGHFSYEFSNHRDVVVDLQGwvTGNgkgliYLTDPQ 1182
Cdd:pfam02816   81 ELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEdDELEQTMQAFSHFTYERSGGQLLVCDLQG--VGN-----LLTDPA 153

                          170       180       190
                   ....*....|....*....|....*....|....
gi 254553408  1183 IHSVDQKDVT-TNFGKRGIFYFFNNQHasCNEIC 1215
Cdd:pfam02816  154 IHTKDGKRFGdTNLGEEGIASFFSTHK--CNKIC 185
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
 990-1216 1.13e-161

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: 480.43  E-value: 1.13e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  990 SNQLQQAHSALLLKYSKKSELWTAQETVVYLGDYLKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYKERKGLRHHFTDVE 1069
Cdd:cd16969     1 PDQLKRAHDALLLKYSKKSGLWTAQETMVYIGDNLQVGKQGKQRNAFWVHFLHQEETLGRYVGKEYKKPKELQYHFNDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1070 RQMTAQHYVTEFNKRLYEQKIPTQIFYIPSTILLILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYGLAYGH 1149
Cdd:cd16969    81 RQMTAQHYVTEFNKRLYEQNIPTQIFFIPSVILLILEDKGIKGCVSVEPYMLGEFVKLTNNTTVKKEEYKATDYGLAYGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553408 1150 FSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKDVTTNFGKRGIFYFFNNQHASCNEICH 1216
Cdd:cd16969   161 FTYEFSNHQDVVVDLQGWVTANGKGLTYLTDPQIHSVVKKSGTTNFGKKGIEYFFNNQHTECNEICR 227
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1007-1215 2.65e-63

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: 213.76  E-value: 2.65e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408   1007 KSELWTAQETVVYLgdYLKVKKKGKQRNAFWVHYL----HQEETLGRYVGKEYKERKgLRHHFTDVERQMTAQHYVTEFN 1082
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLsedgSGTECVAKYFKKEYKNTV-EDRYFEDVEMQMVAKKFAEEFN 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408   1083 KRlyeQKIPTQIFYIPSTILLILeDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYGLAYGHFSYEFSNHRDVVV 1162
Cdd:smart00811   78 QL---KPSPKKIEFLPSYVLELP-DRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTEAPQAFSHFTYERSGGSLLVV 153

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 254553408   1163 DLQGWvtGNgkgliYLTDPQIHSVD-QKDVTTNFGKRGIFYFFNNQHasCNEIC 1215
Cdd:smart00811  154 DLQGV--GD-----LLTDPQIHTEDgFGFGPGNLGEEGIEKFFATHK--CNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1029-1215 1.18e-52

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: 182.53  E-value: 1.18e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  1029 KGKQRNAFWVHYLHQEETLGRYVGKEYKE---RKGLRHHFTDVERQMTAQHYVTEFNK--RLYEQKIPTQIFYIPSTILl 1103
Cdd:pfam02816    2 EGAMRKAFKAKVDPGDESGQNYVAKEFKKivyGVELEYYFEDAQSQALAKELAEEFNAeaRALENFPPKKIEFIPPYVV- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  1104 ILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNE-YKATEYGLAYGHFSYEFSNHRDVVVDLQGwvTGNgkgliYLTDPQ 1182
Cdd:pfam02816   81 ELDPANGKPYYLVEPFLEGNFVKYNSNTGFVSEEdDELEQTMQAFSHFTYERSGGQLLVCDLQG--VGN-----LLTDPA 153

                          170       180       190
                   ....*....|....*....|....*....|....
gi 254553408  1183 IHSVDQKDVT-TNFGKRGIFYFFNNQHasCNEIC 1215
Cdd:pfam02816  154 IHTKDGKRFGdTNLGEEGIASFFSTHK--CNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
 1004-1215 2.55e-46

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: 165.65  E-value: 2.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1004 YSKKSELWTAQETVVYLgDYLKVKKKGKQRNAFWVHYLHQEETlgRYVGKEYKE----RKGLRHHFTDVERQMTAQHYVT 1079
Cdd:cd04515     8 ISVTDLKWTTEETTVRV-AKKKPFAQGAMREAFKAKDLDSKGK--KYVAKRFKRigdpEENLEDLFDELRMQALAQYLAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1080 EFNKRLYEQK-IPTQIFYIPSTILLILE-DRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKAtEYGLAYGHFSYEFSNH 1157
Cdd:cd04515    85 EFNARAKSKNlIAPKINFVDPFVVKLGDrDDPGKVVFLVEPFLEGKFVKYNNNNGMVNDEDLG-ETAQAFSHFTYERSGG 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 254553408 1158 RDVVVDLQGWVTgngkgliYLTDPQIHSVDQKDVT-TNFGKRGIFYFFnNQHAsCNEIC 1215
Cdd:cd04515   164 QLLVTDLQGVGL-------VLTDPQIHTVDGGGFGlGNLGEEGIKRFF-KTHK-CNEIC 213
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
 998-1215 1.02e-31

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: 123.11  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408  998 SALLLKYSKKSELWTAQETVVYLGDylKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYK-ERKGLRHHFTDVERQMTAQH 1076
Cdd:cd16968     1 RAIKHEFDPETGKWTSTATKVKIDP--KPFAEGALREAYHLKDLSAPGPSTLFVAKLSKdPNESRETYFEDVEMQMVCKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1077 YVTEFNkrlyEQKIPTQIFYIPSTiLLILEDRTIKGCISVEPYILGEFVKLSNNTKAVKNEYKATEYglAYGHFSYEFSN 1156
Cdd:cd16968    79 WAEKFN----AKNPPKKVEFLPAW-VLELVDRPPPPLCGVEPFIEGEYVKHNNNFGYVDEDERNTPQ--AFSHFTYEASG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1157 HRDVVVDLQGwVtgngkGLIYlTDPQIHSVDQKDV-TTNFGKRGIFYFFNNqHaSCNEIC 1215
Cdd:cd16968   152 HQLLVVDIQG-V-----GDLY-TDPQIHTIDGKGFgKGNLGQKGIEKFLET-H-KCNAIC 202
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
 1024-1215 9.99e-29

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: 115.52  E-value: 9.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1024 LKVKK----KGKQRNAFWVHYLHQEETlGRYVGKEYKERKGLRHH-----FTDVERQMTAQHYVTEFNKRLYEQKIPTQI 1094
Cdd:cd16970    34 VKIAPppfaKGAERWAYYALDTTSDST-KKVVLKEFKTPGSAQRNsreryLESMEVQTVAAKLAFEFNKLLARAGINKKI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1095 FYIPSTILLILEDRTIKgCISVEPYILGEFVKLSNNTkAVKNEYKAtEYGLAYGHFSYEFSNHRDVVVDLQGwVTGNGKG 1174
Cdd:cd16970   113 TFLEAKVLRVANGDSPQ-YYTMESFLEGEYKKFNNNV-GVVNEDEV-EILQAFSHWTYEASKGYLMVVDLQG-VRTDDDG 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 254553408 1175 LIyLTDPQIHSVDQKDV-TTNFGKRGIFYFFNNqHaSCNEIC 1215
Cdd:cd16970   189 FL-LTDPAIHCTDVLRFgRTNLGKEGIDKFFAT-H-KCNQHC 227
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
 1050-1215 1.03e-23

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: 100.48  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1050 YVGKEYKERKGLRHHFTDVERQMTAQHYVTEFNKrlyeQKIPTQIFYIPSTILLiLEDRTIKGCISVEPYILGEFVKLSN 1129
Cdd:cd16967    65 YVAKRYIEPVDREVYFEDVRLQMDAKLWGEEYNR----HNPPKKVDIMQMCVLE-FVDRPGSPLYHLEHFIEGDYIKYNS 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1130 NTKAVKNE-YKATEYglAYGHFSYEFSNHRDVVVDLQgwvtgnGKGLIYlTDPQIHSVDQKDV-TTNFGKRGIFYFFNNq 1207
Cdd:cd16967   140 NSGFVRDDdIRLTPQ--AFSHFTFERSGHQLIVVDIQ------GVGDLY-TDPQIHTADGEGYgDGNLGLRGMALFFHS- 209


                  ....*...
gi 254553408 1208 HAsCNEIC 1215
Cdd:cd16967   210 HR-CNPIC 216
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 1029-1215 1.55e-17

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: 83.58  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1029 KGKQRNAFWVHYL------HQEETLG-RYVGKEYK----ERKGLRHHFTDVERQMTAQHYVTEFNKRL---YEQKIPtQI 1094
Cdd:cd17508    28 EGAERNVFRCTEIskeggtKTATKIGpRLVAKESRhaedESFDIKFHKKFCKTQSTAQELAERFNKRLralPGGPAP-RV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1095 FYIPSTILLILE-DRTIKGCISVEPYILGEFVKLSNNTKAVK---------------NEYKATEYGLAYGHFSYEFSNHR 1158
Cdd:cd17508   107 KFLPCHVYKTKDvSYRGRAWVLVEKELEGKFTKWNTNAGGVKksiesvgegrgesnsSRLRVDDVPQAFSHFTYEHSGGR 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1159 DVVVDLQGWVTGNGKGLIyLTDPQIHSVDQKDV---TTNFGKRGIFYFFNNqHaSCNEIC 1215
Cdd:cd17508   187 FLVCDLQGVWNATPDGFL-LTDPVIHHVSGKRHrfgATDKGLEGIRNFLRT-H-KCSPLC 243
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 1017-1215 5.04e-12

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: 66.60  E-value: 5.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1017 VVYLGDYLKVKKKGKqrnafwvhylhqeetlgRYVGKEYKERKGLRHHFTDVERQMT--AQHYVTEFNKRLYEQK----- 1089
Cdd:cd17509    43 WVYKGFYTSGERKGQ-----------------ACVVKWFKSGHVFEDDYFDGDIKAVdkALEIVNAFNALNRIDKkikin 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1090 IPT-QIFYIPSTiLLILEDRTIkgcisVEPYILGeFVKLSNNTkAVKNEYKATEYGL-AYGHFSYEFSNHRDVVVDLQGW 1167
Cdd:cd17509   106 VPEvWKFGDGLT-LWWLGRRVL-----IEPFIEN-YEKFNSNS-GWNDDSKGWGEVMqALSHFSYHISGGKYLLCDLQGG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 254553408 1168 VTGNGkglIYLTDPQIHSVDQKDV-TTNFGKRGIFYFFNNqHAsCNEIC 1215
Cdd:cd17509   178 VYKNE---YVLTDPVILSRTGREYgVTDLGPEGIWNFFAN-HK-CNKYC 221
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
 1053-1217 2.09e-09

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: 59.58  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1053 KEYKERKGLRHHFTDVERQMTAQHYVTEFNkrlyeQKIPTQIFYIPSTI-LLILEDRTIKGCISVEPYILGEFVKLSNNT 1131
Cdd:cd16965    81 KIFPESTVLHLCLREIQQQRAAQKLMQRFN-----QVKPSSIPYSPRFLeVFLLYCHSAGQWLTVENNMTGEFRKYNNNN 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1132 -KAVKNEYKATEYGLAYGHFSYEFSNHRDVVVDLQGwVTGNgkgliyLTDPQIHSVDQKDV------TTNFGKRGIFYFF 1204
Cdd:cd16965   156 gDEILPTNTLEETMLAFSHWTYEYTRGELLVLDLQG-VGEN------LTDPSVIKVEDKSSgemvfgPANLGEDAIQNFV 228

                         170
                  ....*....|...
gi 254553408 1205 NNQHasCNEICHR 1217
Cdd:cd16965   229 AKHH--CNSCCRK 239
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
 1067-1217 1.49e-07

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: 53.85  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1067 DVERQMTAQHYVTEFNkrlyeQKIPTQIFYIPSTI-LLILEDRTIKGCISVEPYILGEFVKL-SNNTKAVKNEYKATEYG 1144
Cdd:cd16972    95 EIQQQRAAQKLIYTFN-----QVKPHSIPYTPRFLeVFLIYCHSANQWLTIEKYLTGEFRKYnNNNGDEITPTSLLEETL 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254553408 1145 LAYGHFSYEFSNHRDVVVDLQGwVTGNgkgliyLTDPQIHSVDQKDV------TTNFGKRGIFYFFNNQHasCNEICHR 1217
Cdd:cd16972   170 LAFSHWTYEYTRGELLVLDLQG-VGEN------LTDPSVIKPEDKQSrgmvfgPANLGEDAIRNFIAKHH--CNSCCRK 239
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
 1055-1217 2.95e-07

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: 53.08  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1055 YKERKGLRHHFTDVERQMTAQHYVTEFNkrlyeQKIPTQIFYIPSTI-LLILEDRTIKGCISVEPYILGEFVKLSNNTKa 1133
Cdd:cd16971    83 YKEDTVLHLCLREIQQQRAAQKLTFAFN-----QMKPKSIPYSPRFLeVFLLYCHSAGQWFAVEECMTGEFRKYNNNNG- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553408 1134 vkNEYKAT----EYGLAYGHFSYEFSNHRDVVVDLQGwVTGNgkgliyLTDPQIHSVDQKDVT------TNFGKRGIFYF 1203
Cdd:cd16971   157 --DEIIPTnmleETMLAFSHWTYEYTRGELLVLDLQG-VGEN------LTDPSVIKAGEKRSYdmvfgpANLGEDAIKNF 227

                         170
                  ....*....|....
gi 254553408 1204 FNNQHasCNEICHR 1217
Cdd:cd16971   228 RAKHH--CNSCCRK 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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