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Conserved domains on  [gi|62241011|ref|NP_005154|]
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RAC-alpha serine/threonine-protein kinase [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 719.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594   1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594  81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594 161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 364 EEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594 241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 62241011 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594 321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 4.84e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269947  Cd Length: 107  Bit Score: 225.59  E-value: 4.84e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241   1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                        90       100
                ....*....|....*....|....*...
gi 62241011  84 IERTFHVETPEEREEWTTAIQTVADGLK 111
Cdd:cd01241  80 IERTFHVESEEEREEWMKAIQGVASSLK 107
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-408 4.54e-111

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.80  E-value: 4.54e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS-KGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEEIRFPR---TLGPEAKSLLSGLLK 385
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|...
gi 62241011    386 KDPKQRLGggsedAKEIMQHRFF 408
Cdd:smart00220 237 KDPEKRLT-----AEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 719.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594   1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594  81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594 161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 364 EEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594 241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 62241011 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594 321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 4.84e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 225.59  E-value: 4.84e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241   1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                        90       100
                ....*....|....*....|....*...
gi 62241011  84 IERTFHVETPEEREEWTTAIQTVADGLK 111
Cdd:cd01241  80 IERTFHVESEEEREEWMKAIQGVASSLK 107
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
409-476 1.02e-16

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 74.70  E-value: 1.02e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62241011    409 AGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQdDSMECVDSErrpHFPQFSYSA 476
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDS-PLSGGIQQE---PFRGFSYVF 64
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
6-108 2.20e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 69.11  E-value: 2.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011      6 IVKEGWLHKRGE-YIKTWRPRYFLLKNDgTFIGYKERPQDVD---QREAPLNNFSVaQCQLMKTERPRPNTFIIRCLQWT 81
Cdd:smart00233   1 VIKEGWLYKKSGgGKKSWKKRYFVLFNS-TLLYYKSKKDKKSykpKGSIDLSGCTV-REAPDPDSSKKPHCFEIKTSDRK 78
                           90       100
                   ....*....|....*....|....*..
gi 62241011     82 TVIertFHVETPEEREEWTTAIQTVAD 108
Cdd:smart00233  79 TLL---LQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
6-104 3.67e-14

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 249648  Cd Length: 101  Bit Score: 68.65  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011     6 IVKEGWLHKRG-EYIKTWRPRYFLLKNDgTFIGYKERPqdvDQREAPLNNFSVAQCQLMKTER----PRPNTFIIRCLQW 80
Cdd:pfam00169   1 VIKEGWLLKKGsGGRKSWKKRYFVLFDG-VLLYYKDSK---KSSSRPKGSIPLSGCRVTKVPDsedkKRKNVFEIVTGDR 76
                          90       100
                  ....*....|....*....|....
gi 62241011    81 TTVIertFHVETPEEREEWTTAIQ 104
Cdd:pfam00169  77 ETFL---LQAESEEERKEWIKALR 97
Pkinase_C pfam00433
Protein kinase C terminal domain;
428-477 1.42e-10

Protein kinase C terminal domain;


Pssm-ID: 249854  Cd Length: 47  Bit Score: 56.90  E-value: 1.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 62241011   428 QVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSerrpHFPQFSYSAS 477
Cdd:pfam00433   1 KVKSETDTSNFDPEFTSEPPTLTPPDPTVLSAIDQK----DFRGFTYVNP 46
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-408 4.54e-111

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.80  E-value: 4.54e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGATMKTF 309
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS-KGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    310 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-KLFELILMEEIRFPR---TLGPEAKSLLSGLLK 385
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|...
gi 62241011    386 KDPKQRLGggsedAKEIMQHRFF 408
Cdd:smart00220 237 KDPEKRLT-----AEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
150-408 3.10e-101

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 306.48  E-value: 3.10e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   150 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHtLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 229
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTA-RREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   230 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTF 309
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHS-NGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   310 CGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---DHEKLFELILMEEIRFPR----TLGPEAKSLLS 381
Cdd:pfam00069 159 VGTPEYMAPEVLlGGNGYGPKVDVWSLGVILYELLTGKPPFSGEsilDQLQLIRRILGPPLEFDEpksdSGSEEAKDLIK 238
                         250       260
                  ....*....|....*....|....*..
gi 62241011   382 GLLKKDPKQRLGggsedAKEIMQHRFF 408
Cdd:pfam00069 239 KCLNKDPSKRPT-----AEEILQHPWF 260
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
147-455 5.02e-99

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 303.66  E-value: 5.02e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 226
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  227 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEgikdgATM 306
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHS-KDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VPD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  307 KTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLL 384
Cdd:PTZ00263 171 RTFtlCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62241011  385 KKDPKQRLG---GGSEDAKeimQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFD---EEFTAQMITITPPDQD 455
Cdd:PTZ00263 251 QTDHTKRLGtlkGGVADVK---NHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkypDSPVDRLPPLTAAQQA 324
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
149-435 5.97e-54

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 187.26  E-value: 5.97e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 149 EFEYLKLLGKGTFGKVILVKEKatgRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRLCFVM 227
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 228 EYANGGELFFHL---SRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGH-IKITDFGLCKE----- 298
Cdd:COG0515  78 EYVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLH-SKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLlpdpg 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 299 -GIKDGATMKTFCGTPEYLAPEVLEDN---DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL------------ 362
Cdd:COG0515 157 sTSSIPALPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpsla 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 363 -MEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQ-------HVYEKKLSPPFKPQVTSETD 434
Cdd:COG0515 237 sPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSdllkpddSAPLRLSLPPSLEALISSLN 316

                .
gi 62241011 435 T 435
Cdd:COG0515 317 S 317
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
159-408 9.75e-35

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 130.75  E-value: 9.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  159 GTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVA-HTLTENrvlqnsrHPFLTALKYSFQTHDRLCFVMEYANGGELFF 237
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAK-NFNAIEPMvHQLMKD-------NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  238 HLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD-KDGHIKITDFGLCK----EGIKDGatmktfcgT 312
Cdd:PHA03390  99 LLKKEGKLSEAEVKKIIRQLVEALNDLHK-HNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiigtPSCYDG--------T 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEKLFELILMEE-----IRFPRTLGPEAKSLLSGLLKKD 387
Cdd:PHA03390 170 LDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE-DEDEELDLESLLKrqqkkLPFIKNVSKNANDFVQSMLKYN 248
                        250       260
                 ....*....|....*....|.
gi 62241011  388 PKQRLgggsEDAKEIMQHRFF 408
Cdd:PHA03390 249 INYRL----TNYNEIIKHPFL 265
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
122-410 1.29e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 111.84  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  122 SGSPSDNSGAEEMEVSLAKPkhrvTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEvivAKDEVAHTLT-ENR 200
Cdd:PLN00034  52 SSSSSSSSSSASGSAPSAAK----SLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN---HEDTVRRQICrEIE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  201 VLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL-FFHLSRERVFSeDRARfygaEIVSALDYLHSEKnVVYRDLKLEN 279
Cdd:PLN00034 125 ILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLeGTHIADEQFLA-DVAR----QILSGIAYLHRRH-IVHRDIKPSN 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  280 LMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEV----LEDNDY-GRAVDWWGLGVVMYEMMCGRLPF---YN 351
Cdd:PLN00034 199 LLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERintdLNHGAYdGYAGDIWSLGVSILEFYLGRFPFgvgRQ 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  352 QDHEKLFELILMEEI-RFPRTLGPEAKSLLSGLLKKDPKQRLgggseDAKEIMQHRFFAG 410
Cdd:PLN00034 279 GDWASLMCAICMSQPpEAPATASREFRHFISCCLQREPAKRW-----SAMQLLQHPFILR 333
pknD PRK13184
serine/threonine-protein kinase; Reviewed
147-405 1.30e-18

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 87.90  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  147 MNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKdevahtLTENRVLQNSR------HPFLTALkYSFQTH 220
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENP------LLKKRFLREAKiaadliHPGIVPV-YSICSD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  221 -DRLCFVMEYANGGELFF---------HLSRERVFSEDRARFYGA--EIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI 288
Cdd:PRK13184  74 gDPVYYTMPYIEGYTLKSllksvwqkeSLSKELAEKTSVGAFLSIfhKICATIEYVHS-KGVLHRDLKPDNILLGLFGEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011  289 KITDFG--LCKEGIKD-----GATMKTFC-----------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 350
Cdd:PRK13184 153 VILDWGaaIFKKLEEEdlldiDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62241011  351 NQDHEKlfeLILMEEIRFPRTLGP--EAKSLLSGLLKK----DPKQRLGGGSEDAKEIMQH 405
Cdd:PRK13184 233 RKKGRK---ISYRDVILSPIEVAPyrEIPPFLSQIAMKalavDPAERYSSVQELKQDLEPH 290
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
172-391 1.38e-10

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 62.55  E-value: 1.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    172 TGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF-VMEYANGGELFFHLSRERVFSEDRA 250
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011    251 RFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDG---HIKITDFGL------CKEGIKDGATMKT-FCGTPEYLAPEV 320
Cdd:TIGR03903   82 GRLMLQVLDALACAHN-QGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIgtllpgVRDADVATLTRTTeVLGTPTYCAPEQ 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62241011    321 LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD-HEKLFELILMEEIRFPRTL-GPEAKSLLSGLLKKDPKQR 391
Cdd:TIGR03903  161 LRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQLSPVDVSLPPWIaGHPLGQVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
124-479 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 719.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 124 SPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 203
Cdd:cd05594   1 SPSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 204 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 283
Cdd:cd05594  81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 284 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 363
Cdd:cd05594 161 KDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 364 EEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT 443
Cdd:cd05594 241 EEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFT 320
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 62241011 444 AQMITITPPDQDDSMECVDSERRPHFPQFSYSASGT 479
Cdd:cd05594 321 AQMITITPPDQDDSMETVDNERRPHFPQFSYSASAT 356
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
4-111 4.84e-72

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269947  Cd Length: 107  Bit Score: 225.59  E-value: 4.84e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011   4 VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDvDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTV 83
Cdd:cd01241   1 VSVVKEGWLLKRGEYIKNWRPRYFVLKSDGSFIGYKEKPKP-NQDPPPLNNFSVAECQLMKTEKPKPNTFIIRCLQWTTV 79
                        90       100
                ....*....|....*....|....*...
gi 62241011  84 IERTFHVETPEEREEWTTAIQTVADGLK 111
Cdd:cd01241  80 IERTFHVESEEEREEWMKAIQGVASSLK 107
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
154-477 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 703.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHS-QGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG 393
Cdd:cd05571 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 394 GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEcVDSERRPHFPQFS 473
Cdd:cd05571 240 GGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDRGDLLG-LEEEERPHFEQFS 318

                ....
gi 62241011 474 YSAS 477
Cdd:cd05571 319 YSAS 322
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
154-477 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 691.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGG 233
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 234 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTP 313
Cdd:cd05595  81 ELFFHLSRERVFTEERARFYGAEIVSALEYLHS-RDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 314 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG 393
Cdd:cd05595 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 394 GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFS 473
Cdd:cd05595 240 GGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFS 319

                ....
gi 62241011 474 YSAS 477
Cdd:cd05595 320 YSAS 323
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
133-478 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 613.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 133 EMEVSLAKPKhRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTA 212
Cdd:cd05593   1 EMDASTTHHK-RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 213 LKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITD 292
Cdd:cd05593  80 LKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK-IVYRDLKLENLMLDKDGHIKITD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 293 FGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTL 372
Cdd:cd05593 159 FGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 373 GPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPP 452
Cdd:cd05593 239 SADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 318
                       330       340
                ....*....|....*....|....*...
gi 62241011 453 DQ--DDSMECVDSERRPHFPQFSYSASG 478
Cdd:cd05593 319 EKydEDGMDCMDNERRPHFPQFSYSASG 346
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
154-474 7.79e-161

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 461.30  E-value: 7.79e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05570  81 GDLMFHIQRARRFTEERARFYAAEICLALQFLH-ERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRL 392
Cdd:cd05570 160 PDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 393 GGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQdDSMECVDSErrpHFPQF 472
Cdd:cd05570 240 GCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDS-DLLTNIDQE---EFRGF 315

                ..
gi 62241011 473 SY 474
Cdd:cd05570 316 SY 317
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
154-474 2.93e-153

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 442.14  E-value: 2.93e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 154 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 232
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 233 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGT 312
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHS-LNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 313 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRL 392
Cdd:cd05575 160 PEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 393 GGGsEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMI---TITPPDQDDSMECVdSERRPHF 469
Cdd:cd05575 240 GSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVpasVGKSADSVAVSASV-QEADNAF 317

                ....*
gi 62241011 470 PQFSY 474
Cdd:cd05575 318 DGFSY 322
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
156-408 2.01e-151

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 434.64  E-value: 2.01e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 156 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 235
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 236 FFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEY 315
Cdd:cd05123  81 FSHLSKEGRFPEERARFYAAEIVLALEYLHS-LGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62241011 316 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQR