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Conserved domains on  [gi|1825824977|ref|XP_033094616|]
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alpha-protein kinase 2 isoform X3 [Trachypithecus francoisi]

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 ...
1286-1524 3.81e-169

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: 507.82  E-value: 3.81e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1286 TKGCEEIEFSQLIFKEDFLRDSYFGGRLRGQIATEELHFGEGVHRKAFRSTVMHGLTPVFKPGHACVLKVHNAVAYGTRS 1365
Cdd:cd16974      1 EKGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1366 NDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1445
Cdd:cd16974     81 NDELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825824977 1446 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16974    161 EINVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1201-1273 2.26e-06

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: 47.11  E-value: 2.26e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1825824977  1201 GNVKLSCQFAEiHEDSTICWTKDS-KSIAQVQR--SAGDNSTVSFAIVQASLKDQGLYYCCIKNSYGKVTAEFNLT 1273
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGgKLLAESGRfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
 
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 ...
1286-1524 3.81e-169

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: 507.82  E-value: 3.81e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1286 TKGCEEIEFSQLIFKEDFLRDSYFGGRLRGQIATEELHFGEGVHRKAFRSTVMHGLTPVFKPGHACVLKVHNAVAYGTRS 1365
Cdd:cd16974      1 EKGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1366 NDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1445
Cdd:cd16974     81 NDELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825824977 1446 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16974    161 EINVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1304-1524 3.53e-60

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: 205.28  E-value: 3.53e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977  1304 LRDSYFGGRLRGQIatEELHFGEGVHRKAFRSTVMHGltpvFKPGHACVLKVHNavaygTRSNDELIQRNYKlaaqECYV 1383
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYFE----DVEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977  1384 QNTARYYAKIYAAeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCT 1462
Cdd:smart00811   66 QMVAKKFAEEFNQ----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQA 137
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1825824977  1463 FQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATlAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:smart00811  138 FSHFTYERSGGSLLVVDLQGVGDLLTDPQIHT-EDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1325-1524 5.87e-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: 180.99  E-value: 5.87e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1325 GEGVHRKAFRSTVmhglTPVFKPGHACVLKVHNAVAYGTrsndeliqrNYKLAAQECYVQNTARYYAKIYAAEAQPLEGF 1404
Cdd:pfam02816    1 AEGAMRKAFKAKV----DPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1405 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQKTSGCLLVTDMQG 1482
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1825824977 1483 VGMKLTDVGIATLAKGYKGFkGNCSMTFIDQFKALHQCNKYC 1524
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1201-1273 2.26e-06

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: 47.11  E-value: 2.26e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1825824977  1201 GNVKLSCQFAEiHEDSTICWTKDS-KSIAQVQR--SAGDNSTVSFAIVQASLKDQGLYYCCIKNSYGKVTAEFNLT 1273
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGgKLLAESGRfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
1203-1273 2.58e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.47  E-value: 2.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825824977 1203 VKLSCQFAEiHEDSTICWTKDSKSIAQVQR--SAGDNSTVSFAIVQASLKDQGLYYCCIKNSYGKVTAEFNLT 1273
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
1185-1273 4.23e-03

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: 37.99  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1185 PVLLKKIQAEMFPEHSGNVKLSCQFaEIHEDSTICWTKDSKSIAqvqrSAGDNSTVS-----FAIVQASLKDQGLYYCCI 1259
Cdd:cd05760      1 PVVLKHPASAAEIQPSSRVTLRCHI-DGHPRPTYQWFRDGTPLS----DGQGNYSVSskertLTLRSAGPDDSGLYYCCA 75
                           90
                   ....*....|....
gi 1825824977 1260 KNSYGKVTAEFNLT 1273
Cdd:cd05760     76 HNAFGSVCSSQNFT 89
 
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 ...
1286-1524 3.81e-169

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: 507.82  E-value: 3.81e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1286 TKGCEEIEFSQLIFKEDFLRDSYFGGRLRGQIATEELHFGEGVHRKAFRSTVMHGLTPVFKPGHACVLKVHNAVAYGTRS 1365
Cdd:cd16974      1 EKGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1366 NDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1445
Cdd:cd16974     81 NDELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825824977 1446 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16974    161 EINVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
1286-1524 4.19e-155

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: 470.52  E-value: 4.19e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1286 TKGCEEIEFSQLIFKEDFLRDSYFGGRLRGQIATEELHFGEGVHRKAFRSTVMHGLTPVFKPGHACVLKVHNAVAYGTRS 1365
Cdd:cd16966      1 TEVGEEIEMSPLIFAKDLLDSGYWGDKLFGRIATEELHFGEGVLRKASRSKVIYGLMPIFKSGHTCIIKVHNAIAYGTRN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1366 NDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGK 1445
Cdd:cd16966     81 EDSLIQRNYKLTAQECKVQNTAREYAKIFAAEARPLEGFGEVPEIIPLFLIYRPANNIPYATVEEELIGPFVKYSIRDGK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825824977 1446 EINFLRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
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 ...
1290-1524 1.03e-92

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: 299.75  E-value: 1.03e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1290 EEIEFSQLIFKEDFLRDSYFGGRLRGQIATEELHFGEGVHRKAFRSTVMHGLTPVFKPGHACVLKVHNAVAYGTRSNDEL 1369
Cdd:cd16973      5 EEIEMTPMVFAKGLADSGYWGDKFFGRVMTEEAHIGEGCLRKACRAKVIYGLEPVFESGSTCIIKVRNPIAYGTKNESSL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1370 IQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKEINF 1449
Cdd:cd16973     85 AERNYEITIQECKIQNMAREYCKIFAAEARAVPNFGAVLEIIPLYLIYRPANNIPYATVEEDLKGVFQKYCVLDRTGSLV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1825824977 1450 LRRESEAGQKCCTFQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16973    165 ARTKSEVEQKCCTFQHWIYQWTNGNMLVTDLEGVDWKITNVGIATKSKGYQGLKESCSPKVFEQFISHHQCNYYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1304-1524 3.53e-60

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: 205.28  E-value: 3.53e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977  1304 LRDSYFGGRLRGQIatEELHFGEGVHRKAFRSTVMHGltpvFKPGHACVLKVHNavaygTRSNDELIQRNYKlaaqECYV 1383
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYFE----DVEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977  1384 QNTARYYAKIYAAeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCT 1462
Cdd:smart00811   66 QMVAKKFAEEFNQ----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQA 137
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1825824977  1463 FQHWVYQKTSGCLLVTDMQGVGMKLTDVGIATlAKGYKGFKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:smart00811  138 FSHFTYERSGGSLLVVDLQGVGDLLTDPQIHT-EDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1325-1524 5.87e-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: 180.99  E-value: 5.87e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1325 GEGVHRKAFRSTVmhglTPVFKPGHACVLKVHNAVAYGTrsndeliqrNYKLAAQECYVQNTARYYAKIYAAEAQPLEGF 1404
Cdd:pfam02816    1 AEGAMRKAFKAKV----DPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1405 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQKTSGCLLVTDMQG 1482
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1825824977 1483 VGMKLTDVGIATLAKGYKGFkGNCSMTFIDQFKALHQCNKYC 1524
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
1324-1524 8.36e-32

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: 124.43  E-value: 8.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1324 FGEGVHRKAFRstvmhgLTPVFKPGHACVLKVHNavaygtrsNDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEG 1403
Cdd:cd04515     30 FAQGAMREAFK------AKDLDSKGKKYVAKRFK--------RIGDPEENLEDLFDELRMQALAQYLAKEFNARAKSKNL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1404 FGEVPEIIPIFLIHRPENNIP---YATVEEELIGEFVKYSIRDGKEINflrreSEAGQKCCTFQHWVYQKTSGCLLVTDM 1480
Cdd:cd04515     96 IAPKINFVDPFVVKLGDRDDPgkvVFLVEPFLEGKFVKYNNNNGMVND-----EDLGETAQAFSHFTYERSGGQLLVTDL 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1825824977 1481 QGVGMKLTDVGIATLAKGYKGfKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd04515    171 QGVGLVLTDPQIHTVDGGGFG-LGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1408-1525 2.63e-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: 2.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1408 PEIIPIFLIHRPENNIPYAtVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQKTSGCLLVTDMQGVG 1484
Cdd:cd16971    121 PRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIiptNMLEETMLA------FSHWTYEYTRGELLVLDLQGVG 193
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1485 MKLTDVGIATlakgyKGFKGNCSMTF---------IDQFKALHQCNKYCK 1525
Cdd:cd16971    194 ENLTDPSVIK-----AGEKRSYDMVFgpanlgedaIKNFRAKHHCNSCCR 238
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
1408-1525 7.11e-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: 69.98  E-value: 7.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1408 PEIIPIFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQKTSGCLLVTDMQGVG 1484
Cdd:cd16965    121 PRFLEVFLLYCHSAG-QWLTVENNMTGEFRKYNNNNGDEIlptNTLEETMLA------FSHWTYEYTRGELLVLDLQGVG 193
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1485 MKLTDVGIATLAKgykgfKGNCSMTF---------IDQFKALHQCNKYCK 1525
Cdd:cd16965    194 ENLTDPSVIKVED-----KSSGEMVFgpanlgedaIQNFVAKHHCNSCCR 238
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1408-1525 4.16e-12

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: 67.72  E-value: 4.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1408 PEIIPIFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkCCTFQHWVYQKTSGCLLVTDMQGVGMKL 1487
Cdd:cd16972    121 PRFLEVFLIYCHSAN-QWLTIEKYLTGEFRKYNNNNGDEITPTSLLEET---LLAFSHWTYEYTRGELLVLDLQGVGENL 196
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1825824977 1488 TDVG-IATLAKGYKGF---KGNCSMTFIDQFKALHQCNKYCK 1525
Cdd:cd16972    197 TDPSvIKPEDKQSRGMvfgPANLGEDAIRNFIAKHHCNSCCR 238
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
1320-1524 2.11e-11

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: 64.94  E-value: 2.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1320 EELHFGEGVHRKAFRstvMHGLTpVFKPGHACVLKVhnavAYGTRSNDELIQRNYKLaaqecyvQNTARYYAKIYAAEAQ 1399
Cdd:cd16968     24 DPKPFAEGALREAYH---LKDLS-APGPSTLFVAKL----SKDPNESRETYFEDVEM-------QMVCKKWAEKFNAKNP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1400 PLEgfgevPEIIPIF---LIHRPenNIPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkcctFQHWVYQKTSGCLL 1476
Cdd:cd16968     89 PKK-----VEFLPAWvleLVDRP--PPPLCGVEPFIEGEYVKHNNNFGYVDEDERNTPQA------FSHFTYEASGHQLL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1825824977 1477 VTDMQGVGMKLTDVGIATLAKgyKGF-KGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16968    156 VVDIQGVGDLYTDPQIHTIDG--KGFgKGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1300-1524 1.05e-10

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: 63.55  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1300 KEDFLRDSYFGGRLRGqIATEELHFGEGVHRKAFRstvmhgLTPVFKPGhacvlKVHNAVAYGTRsndeLIQRNYKLAAQ 1379
Cdd:cd17508      3 LERARIYKFLPPGAFG-IAVRKLPFGEGAERNVFR------CTEISKEG-----GTKTATKIGPR----LVAKESRHAED 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1380 E----------CYVQNTARYYAKIYAAEAQPLEGfGEVPEI--IPIFLIHRPENNIPYAT---VEEELIGEFVKY----- 1439
Cdd:cd17508     67 EsfdikfhkkfCKTQSTAQELAERFNKRLRALPG-GPAPRVkfLPCHVYKTKDVSYRGRAwvlVEKELEGKFTKWntnag 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1440 ----SIRDGKEINFLRRESEAGQKCCT--FQHWVYQKTSGCLLVTDMQGV------GMKLTDVGIAT-LAKGY------K 1500
Cdd:cd17508    146 gvkkSIESVGEGRGESNSSRLRVDDVPqaFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHvSGKRHrfgatdK 225
                          250       260
                   ....*....|....*....|....
gi 1825824977 1501 GFKGncsmtfIDQFKALHQCNKYC 1524
Cdd:cd17508    226 GLEG------IRNFLRTHKCSPLC 243
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
1425-1524 5.15e-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: 58.51  E-value: 5.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1425 YATVEEELIGEFVKYSIRDGkeiNFLRRESEAGQkccTFQHWVYQKTSGCLLVTDMQGV-----GMKLTDVGI------- 1492
Cdd:cd16970    130 YYTMESFLEGEYKKFNNNVG---VVNEDEVEILQ---AFSHWTYEASKGYLMVVDLQGVrtdddGFLLTDPAIhctdvlr 203
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1825824977 1493 -ATLAKGYKGfkgncsmtfIDQFKALHQCNKYC 1524
Cdd:cd16970    204 fGRTNLGKEG---------IDKFFATHKCNQHC 227
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
1324-1524 4.60e-08

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: 55.41  E-value: 4.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1324 FGEGVHRKAFRSTVMHGLTPVFKPGHACvlkvhNAVAygTRSNDELIQRNYklaAQECYVQNTARYYAKIYAAEaqpleg 1403
Cdd:cd16967     36 FARGAMRECYRAKKLSNFSHNQDWKHAS-----NYVA--KRYIEPVDREVY---FEDVRLQMDAKLWGEEYNRH------ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1404 fgEVPEIIPIF------LIHRPENniPYATVEEELIGEFVKYSIRDGkeinFLRRESE--AGQkccTFQHWVYQKTSGCL 1475
Cdd:cd16967    100 --NPPKKVDIMqmcvleFVDRPGS--PLYHLEHFIEGDYIKYNSNSG----FVRDDDIrlTPQ---AFSHFTFERSGHQL 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1476 LVTDMQGVGMKLTDVGIATL-AKGYKgfKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd16967    169 IVVDIQGVGDLYTDPQIHTAdGEGYG--DGNLGLRGMALFFHSHRCNPIC 216
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1201-1273 2.26e-06

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: 47.11  E-value: 2.26e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1825824977  1201 GNVKLSCQFAEiHEDSTICWTKDS-KSIAQVQR--SAGDNSTVSFAIVQASLKDQGLYYCCIKNSYGKVTAEFNLT 1273
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGgKLLAESGRfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
1203-1273 2.58e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.47  E-value: 2.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825824977 1203 VKLSCQFAEiHEDSTICWTKDSKSIAQVQR--SAGDNSTVSFAIVQASLKDQGLYYCCIKNSYGKVTAEFNLT 1273
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1463-1524 3.63e-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: 40.79  E-value: 3.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1825824977 1463 FQHWVYQKTSGCLLVTDMQGVGMK----LTDVGIATLAKGYKGfKGNCSMTFIDQFKALHQCNKYC 1524
Cdd:cd17509    157 LSHFSYHISGGKYLLCDLQGGVYKneyvLTDPVILSRTGREYG-VTDLGPEGIWNFFANHKCNKYC 221
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
1185-1273 4.23e-03

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: 37.99  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825824977 1185 PVLLKKIQAEMFPEHSGNVKLSCQFaEIHEDSTICWTKDSKSIAqvqrSAGDNSTVS-----FAIVQASLKDQGLYYCCI 1259
Cdd:cd05760      1 PVVLKHPASAAEIQPSSRVTLRCHI-DGHPRPTYQWFRDGTPLS----DGQGNYSVSskertLTLRSAGPDDSGLYYCCA 75
                           90
                   ....*....|....
gi 1825824977 1260 KNSYGKVTAEFNLT 1273
Cdd:cd05760     76 HNAFGSVCSSQNFT 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1203-1268 5.39e-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: 37.31  E-value: 5.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1825824977 1203 VKLSCQFAEiHEDSTICWTKDSKSIAQVQRSAGDNSTVSFA--IVQASLKDQGLYYCCIKNSYGKVTA 1268
Cdd:cd00096      1 VTLTCSASG-NPPPTITWYKNGKPLPPSSRDSRRSELGNGTltISNVTLEDSGTYTCVASNSAGGSAS 67
 
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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