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Conserved domains on  [gi|2102039144|ref|XP_043745194|]
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alpha-protein kinase 2 isoform X2 [Cervus elaphus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
1773-2007 3.97e-162

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: 496.27  E-value: 3.97e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1773 EEIEFSQLIFREDFLRDSYFGGRLHGQIATEELHFGEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRNNDEL 1852
Cdd:cd16974      5 EEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNNDEL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1853 VQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKEINF 1932
Cdd:cd16974     85 IQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKEINV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102039144 1933 LRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATEAKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16974    165 LRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1684-1756 2.88e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 2.88e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2102039144  1684 GNVKLSCQFAEiHEDSTISWTKDSRSIAQVQRRA---GDNSMVSLAILQAGQKDQGLYYCCIRNSYGKVTAEFNLT 1756
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
P_C super family cl05925
P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P ...
37-135 1.89e-03

P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P gene is a transcriptional regulator of genes encoding enzymes for flavonoid biosynthesis in the pathway leading to the production of a red phlobaphene pigment, and P proteins are homologous to the DNA-binding domain of myb-like transcription factors. All members of this family contain the pfam00249 domain.


The actual alignment was detected with superfamily member pfam06640:

Pssm-ID: 429048  Cd Length: 252  Bit Score: 42.30  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144   37 TYEQESPNHTDEKEHPYKEGEGIASGPPTSADAPSSK---SDGACSRQVSADRDPGAPDSENPSAVKDTRQSEEAGDAAN 113
Cdd:pfam06640   42 AKSKELDDPDSKKPEPESGEAKVASGEPAAAASAASSprhSDGARSAVVDPDPDPNQPDSSSGAGGGSTGEGPCSEDATG 121
                           90       100
                   ....*....|....*....|..
gi 2102039144  114 TEGITDGLPFPNSSDAPGKQDV 135
Cdd:pfam06640  122 PLAALDPIEFGDLWEAESEMDA 143
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
1773-2007 3.97e-162

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: 496.27  E-value: 3.97e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1773 EEIEFSQLIFREDFLRDSYFGGRLHGQIATEELHFGEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRNNDEL 1852
Cdd:cd16974      5 EEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNNDEL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1853 VQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKEINF 1932
Cdd:cd16974     85 IQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKEINV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102039144 1933 LRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATEAKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16974    165 LRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1799-2007 1.65e-58

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: 200.66  E-value: 1.65e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1799 QIATEELHFGEGVHRRAFRSKVLRGltpvFKPGHACVLKVHNavaygTRNNDELVQRNYrlaaQECYVQNTARHYAQIYA 1878
Cdd:smart00811   11 GVKIELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYF----EDVEMQMVAKKFAEEFN 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1879 AeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCTFQHWVYQKTSGC 1957
Cdd:smart00811   78 Q----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQAFSHFTYERSGGS 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1958 LLVTDMQGVGMKLTDVGIATEaKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:smart00811  150 LLVVDLQGVGDLLTDPQIHTE-DGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1808-2007 6.70e-51

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: 178.29  E-value: 6.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1808 GEGVHRRAFRSKVlrglTPVFKPGHACVLKVHNAVAYGTrnndelvqrNYRLAAQECYVQNTARHYAQIYAAEAQPLEGF 1887
Cdd:pfam02816    1 AEGAMRKAFKAKV----DPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1888 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQKTSGCLLVTDMQG 1965
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2102039144 1966 VGMKLTDVGIATEAKGYRGFkGNCSMTFIDQFKALHQCNKYC 2007
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1684-1756 2.88e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 2.88e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2102039144  1684 GNVKLSCQFAEiHEDSTISWTKDSRSIAQVQRRA---GDNSMVSLAILQAGQKDQGLYYCCIRNSYGKVTAEFNLT 1756
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
1686-1756 2.31e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 2.31e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102039144 1686 VKLSCQFAEiHEDSTISWTKDSRSIAQVQR----RAGDNSmvSLAILQAGQKDQGLYYCCIRNSYGKVTAEFNLT 1756
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkvtYEGGTY--TLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
1668-1756 2.76e-04

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 41.84  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1668 PVLLKKIQAEMSPDHSGNVKLSCQFaEIHEDSTISWTKDSRSIAQVQrraGDNSMVS----LAILQAGQKDQGLYYCCIR 1743
Cdd:cd05760      1 PVVLKHPASAAEIQPSSRVTLRCHI-DGHPRPTYQWFRDGTPLSDGQ---GNYSVSSkertLTLRSAGPDDSGLYYCCAH 76
                           90
                   ....*....|...
gi 2102039144 1744 NSYGKVTAEFNLT 1756
Cdd:cd05760     77 NAFGSVCSSQNFT 89
P_C pfam06640
P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P ...
37-135 1.89e-03

P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P gene is a transcriptional regulator of genes encoding enzymes for flavonoid biosynthesis in the pathway leading to the production of a red phlobaphene pigment, and P proteins are homologous to the DNA-binding domain of myb-like transcription factors. All members of this family contain the pfam00249 domain.


Pssm-ID: 429048  Cd Length: 252  Bit Score: 42.30  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144   37 TYEQESPNHTDEKEHPYKEGEGIASGPPTSADAPSSK---SDGACSRQVSADRDPGAPDSENPSAVKDTRQSEEAGDAAN 113
Cdd:pfam06640   42 AKSKELDDPDSKKPEPESGEAKVASGEPAAAASAASSprhSDGARSAVVDPDPDPNQPDSSSGAGGGSTGEGPCSEDATG 121
                           90       100
                   ....*....|....*....|..
gi 2102039144  114 TEGITDGLPFPNSSDAPGKQDV 135
Cdd:pfam06640  122 PLAALDPIEFGDLWEAESEMDA 143
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
1773-2007 3.97e-162

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: 496.27  E-value: 3.97e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1773 EEIEFSQLIFREDFLRDSYFGGRLHGQIATEELHFGEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRNNDEL 1852
Cdd:cd16974      5 EEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNNDEL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1853 VQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKEINF 1932
Cdd:cd16974     85 IQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKEINV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102039144 1933 LRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATEAKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16974    165 LRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
1769-2007 1.48e-146

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: 453.18  E-value: 1.48e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1769 VKVYEEIEFSQLIFREDFLRDSYFGGRLHGQIATEELHFGEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRN 1848
Cdd:cd16966      1 TEVGEEIEMSPLIFAKDLLDSGYWGDKLFGRIATEELHFGEGVLRKASRSKVIYGLMPIFKSGHTCIIKVHNAIAYGTRN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1849 NDELVQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1928
Cdd:cd16966     81 EDSLIQRNYKLTAQECKVQNTAREYAKIFAAEARPLEGFGEVPEIIPLFLIYRPANNIPYATVEEELIGPFVKYSIRDGK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102039144 1929 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATEAKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16966    161 EINFLRSESEAGQKCCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGIATLAKGYQGLKGNCSMTFIDQFAALHQCNKYC 239
Alpha_kinase_ALPK3 cd16973
Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called ...
1769-2007 2.68e-94

Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called muscle alpha-protein kinase (MAK) or myocytic induction/differentiation originator (Midori). Its expression is restricted to fetal and adult heart and adult skeletal muscle, and is localized in the nucleus. It is thought to act as a transcriptional regulator implicated in early cardiac development. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. ALPK3 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: 341223  Cd Length: 239  Bit Score: 305.15  E-value: 2.68e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1769 VKVYEEIEFSQLIFREDFLRDSYFGGRLHGQIATEELHFGEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRN 1848
Cdd:cd16973      1 IEVGEEIEMTPMVFAKGLADSGYWGDKFFGRVMTEEAHIGEGCLRKACRAKVIYGLEPVFESGSTCIIKVRNPIAYGTKN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1849 NDELVQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1928
Cdd:cd16973     81 ESSLAERNYEITIQECKIQNMAREYCKIFAAEARAVPNFGAVLEIIPLYLIYRPANNIPYATVEEDLKGVFQKYCVLDRT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2102039144 1929 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATEAKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16973    161 GSLVARTKSEVEQKCCTFQHWIYQWTNGNMLVTDLEGVDWKITNVGIATKSKGYQGLKESCSPKVFEQFISHHQCNYYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1799-2007 1.65e-58

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: 200.66  E-value: 1.65e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1799 QIATEELHFGEGVHRRAFRSKVLRGltpvFKPGHACVLKVHNavaygTRNNDELVQRNYrlaaQECYVQNTARHYAQIYA 1878
Cdd:smart00811   11 GVKIELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYF----EDVEMQMVAKKFAEEFN 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1879 AeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCTFQHWVYQKTSGC 1957
Cdd:smart00811   78 Q----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQAFSHFTYERSGGS 149
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 2102039144  1958 LLVTDMQGVGMKLTDVGIATEaKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:smart00811  150 LLVVDLQGVGDLLTDPQIHTE-DGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1808-2007 6.70e-51

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: 178.29  E-value: 6.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1808 GEGVHRRAFRSKVlrglTPVFKPGHACVLKVHNAVAYGTrnndelvqrNYRLAAQECYVQNTARHYAQIYAAEAQPLEGF 1887
Cdd:pfam02816    1 AEGAMRKAFKAKV----DPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1888 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQKTSGCLLVTDMQG 1965
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2102039144 1966 VGMKLTDVGIATEAKGYRGFkGNCSMTFIDQFKALHQCNKYC 2007
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
1807-2007 3.08e-31

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: 122.89  E-value: 3.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1807 FGEGVHRRAFRSKVLRGltpvfkPGHACVLKVhnavaygtRNNDELVQRNYRLAAQECYVQNTARHYAQIYAAEAQPLEG 1886
Cdd:cd04515     30 FAQGAMREAFKAKDLDS------KGKKYVAKR--------FKRIGDPEENLEDLFDELRMQALAQYLAKEFNARAKSKNL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1887 FGEVPEIIPIFLIHRPENNIP---YATVEEELIGEFVKYSIRDGKEINflrreSEAGQKCCTFQHWVYQKTSGCLLVTDM 1963
Cdd:cd04515     96 IAPKINFVDPFVVKLGDRDDPgkvVFLVEPFLEGKFVKYNNNNGMVND-----EDLGETAQAFSHFTYERSGGQLLVTDL 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2102039144 1964 QGVGMKLTDVGIATEaKGYRGFKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd04515    171 QGVGLVLTDPQIHTV-DGGGFGLGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1800-2008 4.29e-14

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: 73.88  E-value: 4.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1800 IATEELhfgEGVHRRAFRSKVLRGLTPVFKPGHACVLKVHNAvaygtrnndELVQRNYRLAAQECYVQNTARHYAQIYAA 1879
Cdd:cd16972     35 LSREEM---DGGLRRAMKVVCTWSEDDVLKPGQVFIVKSFLP---------EVVQTWQKIFNNSTVLHLCLREIQQQRAA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1880 EaQPLEGFGEV-PEIIP-------IFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkCCTFQHWVY 1951
Cdd:cd16972    103 Q-KLIYTFNQVkPHSIPytprfleVFLIYCHSAN-QWLTIEKYLTGEFRKYNNNNGDEITPTSLLEET---LLAFSHWTY 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102039144 1952 QKTSGCLLVTDMQGVGMKLTDVG-IATEAKGYRGF---KGNCSMTFIDQFKALHQCNKYCK 2008
Cdd:cd16972    178 EYTRGELLVLDLQGVGENLTDPSvIKPEDKQSRGMvfgPANLGEDAIRNFIAKHHCNSCCR 238
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1800-2008 3.50e-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: 71.19  E-value: 3.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1800 IATEELhfGEGVhRRAFRSKVLRGLTPVFKPGHACVLKVHNAVAYGTRNNDELVQRNYRLAAQECYVQNTARHYAqiYAA 1879
Cdd:cd16971     35 LSKEEM--GGGL-RRALKVVCTWSENDILKSGHLYIIKSFLPEVVNTWSSIYKEDTVLHLCLREIQQQRAAQKLT--FAF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1880 EAQPLEGFGEVPEIIPIFLIHRPENNIPYAtVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQKTSG 1956
Cdd:cd16971    110 NQMKPKSIPYSPRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIiptNMLEETMLA------FSHWTYEYTRG 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102039144 1957 CLLVTDMQGVGMKLTDVGIATEakgyrGFKGNCSMTF---------IDQFKALHQCNKYCK 2008
Cdd:cd16971    183 ELLVLDLQGVGENLTDPSVIKA-----GEKRSYDMVFgpanlgedaIKNFRAKHHCNSCCR 238
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
1891-2008 3.76e-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: 3.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1891 PEIIPIFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQKTSGCLLVTDMQGVG 1967
Cdd:cd16965    121 PRFLEVFLLYCHSAG-QWLTVENNMTGEFRKYNNNNGDEIlptNTLEETMLA------FSHWTYEYTRGELLVLDLQGVG 193
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2102039144 1968 MKLTDVG-IATEAKGYRGF---KGNCSMTFIDQFKALHQCNKYCK 2008
Cdd:cd16965    194 ENLTDPSvIKVEDKSSGEMvfgPANLGEDAIQNFVAKHHCNSCCR 238
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
1803-2007 2.60e-12

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: 68.03  E-value: 2.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1803 EELHFGEGVHRRAFRSKVLRGLtpvfKPGHACVLKVhnavaygTRNNDELVQRNYrlaaQECYVQNTARHYAQIYAAEAQ 1882
Cdd:cd16968     24 DPKPFAEGALREAYHLKDLSAP----GPSTLFVAKL-------SKDPNESRETYF----EDVEMQMVCKKWAEKFNAKNP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1883 PLEgfgevPEIIPIF---LIHRPenNIPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkcctFQHWVYQKTSGCLL 1959
Cdd:cd16968     89 PKK-----VEFLPAWvleLVDRP--PPPLCGVEPFIEGEYVKHNNNFGYVDEDERNTPQA------FSHFTYEASGHQLL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2102039144 1960 VTDMQGVGMKLTDVGIAT-EAKGYrGfKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16968    156 VVDIQGVGDLYTDPQIHTiDGKGF-G-KGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1783-2007 1.15e-11

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: 67.02  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1783 REDFLRDSYFGGRLHGqIATEELHFGEGVHRRAFRskvlrgLTPVFKPGhacvlKVHNAVAYGTRnndeLVQRNYRLAAQ 1862
Cdd:cd17508      3 LERARIYKFLPPGAFG-IAVRKLPFGEGAERNVFR------CTEISKEG-----GTKTATKIGPR----LVAKESRHAED 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1863 E----------CYVQNTARHYAQIYAAEAQPLEGfGEVPEI--IPIFLIHRPENNIPYAT---VEEELIGEFVKY----- 1922
Cdd:cd17508     67 EsfdikfhkkfCKTQSTAQELAERFNKRLRALPG-GPAPRVkfLPCHVYKTKDVSYRGRAwvlVEKELEGKFTKWntnag 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1923 ----SIRDGKEINFLRRESEAGQKCCT--FQHWVYQKTSGCLLVTDMQGV------GMKLTDVGIAT---EAKGY----R 1983
Cdd:cd17508    146 gvkkSIESVGEGRGESNSSRLRVDDVPqaFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHvsgKRHRFgatdK 225
                          250       260
                   ....*....|....*....|....
gi 2102039144 1984 GFKGncsmtfIDQFKALHQCNKYC 2007
Cdd:cd17508    226 GLEG------IRNFLRTHKCSPLC 243
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
1908-2007 4.40e-09

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: 58.89  E-value: 4.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1908 YATVEEELIGEFVKYSIRDGkeiNFLRRESEAGQkccTFQHWVYQKTSGCLLVTDMQGV-----GMKLTDVGI-ATEAK- 1980
Cdd:cd16970    130 YYTMESFLEGEYKKFNNNVG---VVNEDEVEILQ---AFSHWTYEASKGYLMVVDLQGVrtdddGFLLTDPAIhCTDVLr 203
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2102039144 1981 ------GYRGfkgncsmtfIDQFKALHQCNKYC 2007
Cdd:cd16970    204 fgrtnlGKEG---------IDKFFATHKCNQHC 227
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
1807-2007 6.45e-09

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: 58.11  E-value: 6.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1807 FGEGVHRRAFRSKVLRGLTPVFKPGHACvlkvhNAVAygTRNNDELVQRNYrlaAQECYVQNTARHYAQIYAAEaqpleg 1886
Cdd:cd16967     36 FARGAMRECYRAKKLSNFSHNQDWKHAS-----NYVA--KRYIEPVDREVY---FEDVRLQMDAKLWGEEYNRH------ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1887 fgEVPEIIPIF------LIHRPENniPYATVEEELIGEFVKYSIRDGkeinFLRRESE--AGQkccTFQHWVYQKTSGCL 1958
Cdd:cd16967    100 --NPPKKVDIMqmcvleFVDRPGS--PLYHLEHFIEGDYIKYNSNSG----FVRDDDIrlTPQ---AFSHFTFERSGHQL 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1959 LVTDMQGVGMKLTDVGIATE-AKGYRgfKGNCSMTFIDQFKALHQCNKYC 2007
Cdd:cd16967    169 IVVDIQGVGDLYTDPQIHTAdGEGYG--DGNLGLRGMALFFHSHRCNPIC 216
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1684-1756 2.88e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 2.88e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2102039144  1684 GNVKLSCQFAEiHEDSTISWTKDSRSIAQVQRRA---GDNSMVSLAILQAGQKDQGLYYCCIRNSYGKVTAEFNLT 1756
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
1686-1756 2.31e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 2.31e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2102039144 1686 VKLSCQFAEiHEDSTISWTKDSRSIAQVQR----RAGDNSmvSLAILQAGQKDQGLYYCCIRNSYGKVTAEFNLT 1756
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkvtYEGGTY--TLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
1668-1756 2.76e-04

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 41.84  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144 1668 PVLLKKIQAEMSPDHSGNVKLSCQFaEIHEDSTISWTKDSRSIAQVQrraGDNSMVS----LAILQAGQKDQGLYYCCIR 1743
Cdd:cd05760      1 PVVLKHPASAAEIQPSSRVTLRCHI-DGHPRPTYQWFRDGTPLSDGQ---GNYSVSSkertLTLRSAGPDDSGLYYCCAH 76
                           90
                   ....*....|...
gi 2102039144 1744 NSYGKVTAEFNLT 1756
Cdd:cd05760     77 NAFGSVCSSQNFT 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1684-1751 1.07e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.79  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102039144 1684 GNVKLSCQfAEIHEDSTISWTKDSRSIAQVQRRAGDNSMVSLAILQAGQKDQGLYYCCIRNSYGKVTA 1751
Cdd:cd20952     15 GTVVLNCQ-ATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATW 81
P_C pfam06640
P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P ...
37-135 1.89e-03

P protein C-terminus; This family represents the C-terminus of plant P proteins. The maize P gene is a transcriptional regulator of genes encoding enzymes for flavonoid biosynthesis in the pathway leading to the production of a red phlobaphene pigment, and P proteins are homologous to the DNA-binding domain of myb-like transcription factors. All members of this family contain the pfam00249 domain.


Pssm-ID: 429048  Cd Length: 252  Bit Score: 42.30  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102039144   37 TYEQESPNHTDEKEHPYKEGEGIASGPPTSADAPSSK---SDGACSRQVSADRDPGAPDSENPSAVKDTRQSEEAGDAAN 113
Cdd:pfam06640   42 AKSKELDDPDSKKPEPESGEAKVASGEPAAAASAASSprhSDGARSAVVDPDPDPNQPDSSSGAGGGSTGEGPCSEDATG 121
                           90       100
                   ....*....|....*....|..
gi 2102039144  114 TEGITDGLPFPNSSDAPGKQDV 135
Cdd:pfam06640  122 PLAALDPIEFGDLWEAESEMDA 143
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1686-1751 2.17e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.46  E-value: 2.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2102039144 1686 VKLSCQFAEiHEDSTISWTKDSRSIAQVQRRAGDNSMV--SLAILQAGQKDQGLYYCCIRNSYGKVTA 1751
Cdd:cd00096      1 VTLTCSASG-NPPPTITWYKNGKPLPPSSRDSRRSELGngTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1946-2007 5.44e-03

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: 40.41  E-value: 5.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102039144 1946 FQHWVYQKTSGCLLVTDMQGVGMK----LTD-VGIATEAKGY----RGFKGncsmtfIDQFKALHQCNKYC 2007
Cdd:cd17509    157 LSHFSYHISGGKYLLCDLQGGVYKneyvLTDpVILSRTGREYgvtdLGPEG------IWNFFANHKCNKYC 221
 
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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