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Conserved domains on  [gi|1716990059|ref|XP_030072657|]
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phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform [Microcaecilia unicolor]

Protein Classification

phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform( domain architecture ID 18341684)

phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform phosphorylates PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 732-1098 0e+00

Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility. It associates with one of two regulatory subunits, p101 and p84, and is activated by G-protein-coupled receptors (GPCRs) by direct binding to their betagamma subunits. It contains an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


:

Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 763.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  732 LHDFMKQVQVTEMLHKVTMEIKSISAEKYDVTSQVITQLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKK 811
Cdd:cd00894      1 LHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLRAGALVIEKCKVMASKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  812 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTI 891
Cdd:cd00894     81 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  892 AKIQQSTVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHI 971
Cdd:cd00894    161 AKIQQSTVGNTGAFKDEVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  972 LGNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 1051
Cdd:cd00894    241 LGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 320

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1716990059 1052 EYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLVLGIK 1098
Cdd:cd00894    321 EYIRDALTVGKSEEDAKKHFLDQIEVCRDKGWTVQFNWFLHLVLGIK 367
PIK3CG_ABD pfam19710
PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from ...
 1-192 1.12e-123

PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from PI3-kinase catalytic subunit gamma (PIK3CG, also known as p110 catalytic subunit gamma) which contains the adaptor-binding domain (ABD). This is a globular domain with an alpha/beta sandwich topology, common to all catalytic subunits of PIK3s, and it is similar to ubiquitin-like domains. This domain interacts with the regulatory subunit of the p101 type.


:

Pssm-ID: 466155  Cd Length: 195  Bit Score: 376.80  E-value: 1.12e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059    1 MELENYEQPVVLREENKHRRRRMRPHSAASNLSSTELISIEFFLPTVSKLTKTQDTLVLEIAGNCTVEQMKAQVWMRAIE 80
Cdd:pfam19710    4 MQLSDHEQPVVMREENRRRRRRMKKAFTSASSSSMELISIEFVLPTSNKNTKTPDTLLLEVAGNWTVEQVKAQVWLRAVE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   81 TNLNSDFYHKLTPDHFLLHYQKKGQWYEIYDKHQVIQTLDCILYWKVLQKKVGKIHIVEKQKMTEEVLEFQKQLNYLIGY 160
Cdd:pfam19710   84 TNLCPDFYQKFSPDQFILLYQKKGQWYEIYDKHQVFQTLDCIRYWKALQKDVGKIHLVQRPQPSEESLQYQRQLNYLIGY 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1716990059  161 DVTDVSNVHDDELEFTRRRLVTPRVIELASRD 192
Cdd:pfam19710  164 DVTDVSNVHDDELEFTRRKLVTPRMIELSDRD 195
C2_PI3K_class_I_gamma cd08399
C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 350-530 1.38e-110

C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, gamma isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


:

Pssm-ID: 176044  Cd Length: 178  Bit Score: 341.51  E-value: 1.38e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  350 FTISLWDCNRKFRVKVIGIDIPVLPRNTELMVFVEANIQHGQQLLAQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALL 429
Cdd:cd08399      1 FTVSLWDCDRKFRVKILGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNTWLEFDIKIKDLPKGALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  430 NLQIYCGKSPSLTTKTNVQphdTLSSDSKCKNQLLYYVNLLLIDHRFLLRQGDYVLHMWKIPGKGEEQGSINADKLTSAT 509
Cdd:cd08399     81 NLQIYCGKAPALSSKKSAE---SPSSESKGKHQLLYYVNLLLIDHRFLLRTGEYVLHMWQISGKGEDQGSVNADKLTSAT 157

                          170       180
                   ....*....|....*....|.
gi 1716990059  510 NPDKETSMAISIVLDRYCHPI 530
Cdd:cd08399    158 NPDKENSMSISILLDNYCHPV 178
PI3Ka_I cd00872
Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all ...
 552-728 8.04e-86

Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3K class I prefer phosphoinositol (4,5)-bisphosphate as a substrate. Mammalian members interact with active Ras. They form heterodimers with adapter molecules linking them to different signaling pathways.


:

Pssm-ID: 238444  Cd Length: 171  Bit Score: 274.58  E-value: 8.04e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  552 NQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAkkeawDRSSLDVGLTM 631
Cdd:cd00872      1 NEEREQLEAIIARDPLSELTEEDKELLWKLRHECRKKPQALPKLLLSVKWNKRDDVAQMYQLLK-----RWPKLKPEQAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  632 QLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIAQSMH 711
Cdd:cd00872     76 ELLDCNFPDEHVREFAVRCLEKLSDDELLQYLLQLVQVLKYEPYHDSDLVRFLLKRALRNQRIGHFFFWHLRSEMHNPSV 155

                          170
                   ....*....|....*..
gi 1716990059  712 yQQRFAVLLEAYLRGCG 728
Cdd:cd00872    156 -SQRFGLLLEAYLRGCG 171
PI3K_rbd super family cl02484
PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding ...
 203-312 1.13e-25

PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding pfam00788 domains (unpublished observation).


The actual alignment was detected with superfamily member smart00144:

Pssm-ID: 413336  Cd Length: 108  Bit Score: 102.41  E-value: 1.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   203 TSKPLPEYMFKKITSSNVFIVIHR--GTTSQTIKVSIDDTPNMILQTFFTKiakKKSLLDiPEDHSELDFVLRVCGRDEY 280
Cdd:smart00144    1 TSPSVPEPLPLKTIANKILIVVHLekDQQTKTLKVNPNCTPDSVLAQAFTK---MLSLHD-QVDPTSEDYILKVCGRDEY 76

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1716990059   281 IIGDTPIRDFHWIRECHKNGEEIHLVLDTPPD 312
Cdd:smart00144   77 LLGDHPLGSFEYIRNCLKNGTEPHLVLMTLSA 108
 
Name Accession Description Interval E-value
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 732-1098 0e+00

Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility. It associates with one of two regulatory subunits, p101 and p84, and is activated by G-protein-coupled receptors (GPCRs) by direct binding to their betagamma subunits. It contains an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 763.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  732 LHDFMKQVQVTEMLHKVTMEIKSISAEKYDVTSQVITQLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKK 811
Cdd:cd00894      1 LHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLRAGALVIEKCKVMASKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  812 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTI 891
Cdd:cd00894     81 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  892 AKIQQSTVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHI 971
Cdd:cd00894    161 AKIQQSTVGNTGAFKDEVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  972 LGNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 1051
Cdd:cd00894    241 LGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 320

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1716990059 1052 EYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLVLGIK 1098
Cdd:cd00894    321 EYIRDALTVGKSEEDAKKHFLDQIEVCRDKGWTVQFNWFLHLVLGIK 367
PIK3CG_ABD pfam19710
PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from ...
 1-192 1.12e-123

PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from PI3-kinase catalytic subunit gamma (PIK3CG, also known as p110 catalytic subunit gamma) which contains the adaptor-binding domain (ABD). This is a globular domain with an alpha/beta sandwich topology, common to all catalytic subunits of PIK3s, and it is similar to ubiquitin-like domains. This domain interacts with the regulatory subunit of the p101 type.


Pssm-ID: 466155  Cd Length: 195  Bit Score: 376.80  E-value: 1.12e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059    1 MELENYEQPVVLREENKHRRRRMRPHSAASNLSSTELISIEFFLPTVSKLTKTQDTLVLEIAGNCTVEQMKAQVWMRAIE 80
Cdd:pfam19710    4 MQLSDHEQPVVMREENRRRRRRMKKAFTSASSSSMELISIEFVLPTSNKNTKTPDTLLLEVAGNWTVEQVKAQVWLRAVE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   81 TNLNSDFYHKLTPDHFLLHYQKKGQWYEIYDKHQVIQTLDCILYWKVLQKKVGKIHIVEKQKMTEEVLEFQKQLNYLIGY 160
Cdd:pfam19710   84 TNLCPDFYQKFSPDQFILLYQKKGQWYEIYDKHQVFQTLDCIRYWKALQKDVGKIHLVQRPQPSEESLQYQRQLNYLIGY 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1716990059  161 DVTDVSNVHDDELEFTRRRLVTPRVIELASRD 192
Cdd:pfam19710  164 DVTDVSNVHDDELEFTRRKLVTPRMIELSDRD 195
C2_PI3K_class_I_gamma cd08399
C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 350-530 1.38e-110

C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, gamma isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176044  Cd Length: 178  Bit Score: 341.51  E-value: 1.38e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  350 FTISLWDCNRKFRVKVIGIDIPVLPRNTELMVFVEANIQHGQQLLAQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALL 429
Cdd:cd08399      1 FTVSLWDCDRKFRVKILGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNTWLEFDIKIKDLPKGALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  430 NLQIYCGKSPSLTTKTNVQphdTLSSDSKCKNQLLYYVNLLLIDHRFLLRQGDYVLHMWKIPGKGEEQGSINADKLTSAT 509
Cdd:cd08399     81 NLQIYCGKAPALSSKKSAE---SPSSESKGKHQLLYYVNLLLIDHRFLLRTGEYVLHMWQISGKGEDQGSVNADKLTSAT 157

                          170       180
                   ....*....|....*....|.
gi 1716990059  510 NPDKETSMAISIVLDRYCHPI 530
Cdd:cd08399    158 NPDKENSMSISILLDNYCHPV 178
PI3Ka_I cd00872
Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all ...
 552-728 8.04e-86

Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3K class I prefer phosphoinositol (4,5)-bisphosphate as a substrate. Mammalian members interact with active Ras. They form heterodimers with adapter molecules linking them to different signaling pathways.


Pssm-ID: 238444  Cd Length: 171  Bit Score: 274.58  E-value: 8.04e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  552 NQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAkkeawDRSSLDVGLTM 631
Cdd:cd00872      1 NEEREQLEAIIARDPLSELTEEDKELLWKLRHECRKKPQALPKLLLSVKWNKRDDVAQMYQLLK-----RWPKLKPEQAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  632 QLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIAQSMH 711
Cdd:cd00872     76 ELLDCNFPDEHVREFAVRCLEKLSDDELLQYLLQLVQVLKYEPYHDSDLVRFLLKRALRNQRIGHFFFWHLRSEMHNPSV 155

                          170
                   ....*....|....*..
gi 1716990059  712 yQQRFAVLLEAYLRGCG 728
Cdd:cd00872    156 -SQRFGLLLEAYLRGCG 171
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 833-1049 4.26e-79

Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in a variety of processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced, the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 259.15  E-value: 4.26e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   833 IIFKHGDDLRQDMLILQILRIMESIWEAEA----LDLCLLPYGCISTGNKIGMIEIVKDATTIAKIQ------------- 895
Cdd:smart00146    1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDKetrrRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILkeyrkqkgkvldl 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   896 -----------QSTVGNTGAFKDEVLNQWLKEKCPVE-EKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNL 963
Cdd:smart00146   81 rsqtatrlkklELFLEATGKFPDPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGHL 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   964 FHIDFGHILGNYKSFLGiNKERVPFVLTPDFLYVMGTSGkktsqHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMP 1043
Cdd:smart00146  161 FHIDFGFILGNGPKLFG-FPERVPFRLTPEMVDVMGDSG-----YFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLP 234


                    ....*.
gi 1716990059  1044 QLTSKE 1049
Cdd:smart00146  235 DWRSGK 240
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 547-735 1.87e-74

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 395488  Cd Length: 185  Bit Score: 243.78  E-value: 1.87e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  547 RTEMPNQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAKkeaWDRssLD 626
Cdd:pfam00613    2 DLKPNEKERKELEAILAYDPLSKLTAEEKDLIWKFRYYLMLVPKALTKLLLSVKWSDLSEVAEALSLLLK---WAP--ID 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  627 VGLTMQLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEI 706
Cdd:pfam00613   77 PVDALELLDPKFPDPEVRQYAVKCLESASDDELLFYLLQLVQALKYEPFHDSYLSRFLLQRALKNRRIGHFFFWYLKSEI 156

                          170       180
                   ....*....|....*....|....*....
gi 1716990059  707 AQSmHYQQRFAVLLEAYLRGCGKAMLHDF 735
Cdd:pfam00613  157 HDE-EVSPRFGSLLELYLRSCGTSLLGLN 184
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 551-735 1.15e-72

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 214537  Cd Length: 184  Bit Score: 239.08  E-value: 1.15e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   551 PNQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIK-HPKAYPKLLASVKWGHQETVAKTYQLLAKkeaWDrsSLDVGL 629
Cdd:smart00145    4 DIEEREQLEAILKLDPTYELTEEEKDLIWKFRHYYLTnNPKALPKFLLSVKWSDADEVAQALSLLLS---WA--PLDPED 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   630 TMQLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIaQS 709
Cdd:smart00145   79 ALELLDPKFPDPFVRAYAVKRLESASDEELLLYLLQLVQALKYEPYLDSALARFLLERALANQRLGHFFYWYLKSEL-HD 157

                           170       180
                    ....*....|....*....|....*.
gi 1716990059   710 MHYQQRFAVLLEAYLRGCGKAMLHDF 735
Cdd:smart00145  158 PHVSIRFGLLLEAYLRGCGTHLKELL 183
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 831-1047 1.00e-70

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 235.69  E-value: 1.00e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  831 IGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLL-PYGCISTGNKIGMIEIVKDATTIAKIQQ----STVGNTGAF 905
Cdd:pfam00454    2 YGGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRRLkPYSVIPLGPKCGIIEWVPNSETLAYILDeygeNGVPPTAMV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  906 KD-----------------------EVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMI-TESG 961
Cdd:pfam00454   82 KIlhsalnypklklefesrislppkVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVdKTTG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  962 NLFHIDFGHILGNYKSFLGINkERVPFVLTPDFLYVMGTSGkktsqHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTG 1041
Cdd:pfam00454  162 KLFHIDFGLCLPDAGKDLPFP-EKVPFRLTREMVYAMGPSG-----DEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235


                   ....*.
gi 1716990059 1042 MPQLTS 1047
Cdd:pfam00454  236 LPDWSI 241
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
809-1076 2.09e-40

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 163.42  E-value: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  809 SKKKPLWLEFKCADptalsNETIGIIFKHGDDLRQDMLILQILRIMESIW----EAEALDLCLLPYGCISTGNKIGMIEI 884
Cdd:COG5032   1780 HLQRPRRLTIRGSD-----GKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEW 1854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  885 VKDATTIAKI------------------QQSTVGNTGAFKDE-----------VLNQWLKEKCPVEEKFCASVERFVYSC 935
Cdd:COG5032   1855 VPNSDTLHSIlreyhkrknisidqekklAARLDNLKLLLKDEfftkatlksppVLYDWFSESFPNPEDWLTARTNFARSL 1934

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  936 AGYCVATYVLGIGDRHNDNIMITE-SGNLFHIDFGHILGNYKSFLGINkERVPFVLTPDFLYVMGTSGKKTSqhfhkFED 1014
Cdd:COG5032   1935 AVYSVIGYILGLGDRHPGNILIDRsSGHVIHIDFGFILFNAPGRFPFP-EKVPFRLTRNIVEAMGVSGVEGS-----FRE 2008

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716990059 1015 VCVKAYLALRHHTNLLIILFSMML------------MTGMPQLTSKEDIEYIRDALTvgrsEDEAKRHFLDQIE 1076
Cdd:COG5032   2009 LCETAFRALRKNADSLMNVLELFVrdpliewrrlpcFREIQNNEIVNVLERFRLKLS----EKDAEKFVDLLIN 2078
PI3K_rbd smart00144
PI3-kinase family, Ras-binding domain; Certain members of the PI3K family possess Ras-binding ...
 203-312 1.13e-25

PI3-kinase family, Ras-binding domain; Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding RA domains (unpublished observation).


Pssm-ID: 197540  Cd Length: 108  Bit Score: 102.41  E-value: 1.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   203 TSKPLPEYMFKKITSSNVFIVIHR--GTTSQTIKVSIDDTPNMILQTFFTKiakKKSLLDiPEDHSELDFVLRVCGRDEY 280
Cdd:smart00144    1 TSPSVPEPLPLKTIANKILIVVHLekDQQTKTLKVNPNCTPDSVLAQAFTK---MLSLHD-QVDPTSEDYILKVCGRDEY 76

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1716990059   281 IIGDTPIRDFHWIRECHKNGEEIHLVLDTPPD 312
Cdd:smart00144   77 LLGDHPLGSFEYIRNCLKNGTEPHLVLMTLSA 108
PI3K_C2 smart00142
Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.
 349-444 3.74e-23

Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.


Pssm-ID: 214536  Cd Length: 100  Bit Score: 95.11  E-value: 3.74e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   349 VFTISLWDCNRKFRVKVIGIDIPVLPRNTELM-VFVEANIQHGQQLL-AQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKG 426
Cdd:smart00142    1 VKIESLWDCDRNLVITIALIHGIPLNWSRDYSdLYVEIQLYHGGKLLcLPVSTSYKPFFPSVKWNEWLTFPIQISDLPRE 80

                            90
                    ....*....|....*...
gi 1716990059   427 ALLNLQIYCGKSPSLTTK 444
Cdd:smart00142   81 ARLCITIYAVKNPSKGSE 98
PI3K_rbd pfam00794
PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding ...
 203-312 5.62e-23

PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding pfam00788 domains (unpublished observation).


Pssm-ID: 395642  Cd Length: 106  Bit Score: 94.67  E-value: 5.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  203 TSKPLPEYMfKKITSSNVFIVIH--RGTTSQTIKVSIDDTPNMILQTFFTKiakKKSLLDIPEdhSELDFVLRVCGRDEY 280
Cdd:pfam00794    1 ASTVSPEPL-PKLINNKLLISVHleGDQMTKTFTCNPNSTPGSLIAQALTK---KLSVHTQGD--VTDDYVLKVCGRDEY 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1716990059  281 IIGDTPIRDFHWIRECHKNGEEIHLVLDTPPD 312
Cdd:pfam00794   75 LLGDHPLGQFEYIRNCLKSGREPHLTLVEQSS 106
PI3K_C2 pfam00792
Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 ...
 381-488 4.12e-10

Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 domain. Outlier of pfam00168 family.


Pssm-ID: 395640  Cd Length: 136  Bit Score: 58.92  E-value: 4.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  381 VFVEANIQHGQQLLAQR-RTTCKPF-TEEVLWNTWLDFDIKIKDLPKGALLNLQIYCGKSPSLTTKtnvqphdtlssdsk 458
Cdd:pfam00792    5 LYVECQLYHGGKPLCLPvSTRYVPFsNSSIKWNEWITFPIQISDLPRSARLCITIWDVSGPEKSFV-------------- 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1716990059  459 cknqLLYYVNLLLIDHRFLLRQGDYVLHMW 488
Cdd:pfam00792   71 ----PIGWVNTSLFDKKGILRQGKQKLRLW 96
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 847-979 2.01e-03

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 42.38  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  847 ILQILrIMESIWEAEALDLCLLPYGCIStgnkiGMIEivkdattiaKIQQSTVGNTGAFkdEVLNQWLKEKCPVEEKFCA 926
Cdd:PTZ00303  1073 LLQML-LSSEIGNAEMLDYSVLPLSCDS-----GLIE---------KAEGRELSNLDNM--DIASYVLYRGTRSCINFLA 1135

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1716990059  927 SVERFVyscagycVATYVLGIGDRHNDNIMITESGNLFHIDFGHILGNyKSFL 979
Cdd:PTZ00303  1136 SAKLFL-------LLNYIFSIGDRHKGNVLIGTNGALLHIDFRFIFSE-KTFV 1180
 
Name Accession Description Interval E-value
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 732-1098 0e+00

Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility. It associates with one of two regulatory subunits, p101 and p84, and is activated by G-protein-coupled receptors (GPCRs) by direct binding to their betagamma subunits. It contains an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 763.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  732 LHDFMKQVQVTEMLHKVTMEIKSISAEKYDVTSQVITQLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKK 811
Cdd:cd00894      1 LHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLRAGALVIEKCKVMASKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  812 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTI 891
Cdd:cd00894     81 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  892 AKIQQSTVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHI 971
Cdd:cd00894    161 AKIQQSTVGNTGAFKDEVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  972 LGNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 1051
Cdd:cd00894    241 LGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDI 320

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1716990059 1052 EYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLVLGIK 1098
Cdd:cd00894    321 EYIRDALTVGKSEEDAKKHFLDQIEVCRDKGWTVQFNWFLHLVLGIK 367
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 732-1094 0e+00

Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. In vitro, they can also phosphorylate the substrates PtdIns and PtdIns(4)P. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270709 [Multi-domain]  Cd Length: 363  Bit Score: 570.73  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  732 LHDFMKQVQVTEMLHKVTMEIKSISAEKydvtSQVITQLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKK 811
Cdd:cd05165      1 LKSLSRQVEALNKLKKLSDILKEKKKSK----EKVKKLLKECLKQKFYDEALQNFQSPLNPSHKLGELIIEKCKVMDSKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  812 KPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTI 891
Cdd:cd05165     77 RPLWLVFENADPLALSGEDIKIIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLSTGDNVGLIEVVRNAKTI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  892 AKIQQSTVGN-TGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGH 970
Cdd:cd05165    157 ANIQKKKGKVaTLAFNKDSLHKWLKEKNKTGEKYDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKENGQLFHIDFGH 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  971 ILGNYKSFLGINKERVPFVLTPDFLYVMGT-SGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKE 1049
Cdd:cd05165    237 FLGNFKKKFGIKRERVPFVLTHDFVYVIARgQDNTKSEEFQEFQELCEKAYLILRRHGNLFISLFSMMLSTGIPELTSVK 316

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1716990059 1050 DIEYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLV 1094
Cdd:cd05165    317 DIEYLRKTLALDKTEEEALKYFRKKFNEALKGSWTTKVNWFFHNV 361
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 733-1080 5.26e-178

Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class II PI3Ks comprise three catalytic isoforms that do not associate with any regulatory subunits. They selectively use PtdIns as a susbtrate to produce PtsIns(3)P. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270624 [Multi-domain]  Cd Length: 334  Bit Score: 523.67  E-value: 5.26e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  733 HDFMKQVQVTEMLHKVTMEIKSISAEKydvtsqVITQLRQKLDKMQssnFPESFRVPYDPGLRAGTLVVEKCKVMASKKK 812
Cdd:cd00891      2 EELLKQVKVLDELKEIAKKIKEEPSEE------RKEVLEKLLQKLE---LPKKFTLPLDPRMEVKGLIVEKCKVMDSKKL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  813 PLWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIA 892
Cdd:cd00891     73 PLWLVFKNADPGG---DPIKVIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIEVVPNSETTA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  893 KIQQSTVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHIL 972
Cdd:cd00891    150 AIQKKYGGFGAAFKDTPISNWLKKHNPTEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVTKSGHLFHIDFGHFL 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  973 GNYKSFLGINKERVPFVLTPDFLYVMGtsGKKtSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIE 1052
Cdd:cd00891    230 GNFKKKFGIKRERAPFVFTPEMAYVMG--GED-SENFQKFEDLCCKAYNILRKHGNLLINLFSLMLSAGIPELQSIEDIE 306

                          330       340
                   ....*....|....*....|....*...
gi 1716990059 1053 YIRDALTVGRSEDEAKRHFLDQIEICRD 1080
Cdd:cd00891    307 YLRDALQLDLSDEEAAEHFRKLIHESLN 334
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 733-1092 2.51e-127

Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. They are activated by a variety of stimuli including chemokines, cytokines, lysophosphatidic acid (LPA), insulin, and tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270710 [Multi-domain]  Cd Length: 352  Bit Score: 392.42  E-value: 2.51e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  733 HDFMKQVQVTEMLHKVTMEIKSISAEKYDVTsqvitqLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKKK 812
Cdd:cd05166      2 EEFLKQHVLVQALTSIAEKVKSAKDSARENA------LRRELEQLASFLLENSFRLPLDPALEVTGVDVRSCSYFNSNAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  813 PLWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIA 892
Cdd:cd05166     76 PLKLVFRNADPRA---EPISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRGMVELVPEAETLR 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  893 KIQQStVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHIL 972
Cdd:cd05166    153 EIQTE-HGLTGSFKDRPLADWLQKHNPSELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLKTSGHLFHIDFGKFL 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  973 GNYKSFLGINKERVPFVLTPDFLYVMgTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSkEDIE 1052
Cdd:cd05166    232 GDAQMFGNFKRDRVPFVLTSDMAYVI-NGGDKPSSRFQLFVDLCCQAFNIIRKNSNLLLNLLSLMLSSGIPGVTQ-DDLR 309

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1716990059 1053 YIRDALTVGRSEDEAKRHFLDQIEICRdKGWTVQFNWFLH 1092
Cdd:cd05166    310 YVQDALLPELTDAEATAHFTRMIEESL-SSKFTQLNFFIH 348
PIK3CG_ABD pfam19710
PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from ...
 1-192 1.12e-123

PIK3 catalytic subunit gamma adaptor-binding domain; This is the N-terminal domain from PI3-kinase catalytic subunit gamma (PIK3CG, also known as p110 catalytic subunit gamma) which contains the adaptor-binding domain (ABD). This is a globular domain with an alpha/beta sandwich topology, common to all catalytic subunits of PIK3s, and it is similar to ubiquitin-like domains. This domain interacts with the regulatory subunit of the p101 type.


Pssm-ID: 466155  Cd Length: 195  Bit Score: 376.80  E-value: 1.12e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059    1 MELENYEQPVVLREENKHRRRRMRPHSAASNLSSTELISIEFFLPTVSKLTKTQDTLVLEIAGNCTVEQMKAQVWMRAIE 80
Cdd:pfam19710    4 MQLSDHEQPVVMREENRRRRRRMKKAFTSASSSSMELISIEFVLPTSNKNTKTPDTLLLEVAGNWTVEQVKAQVWLRAVE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   81 TNLNSDFYHKLTPDHFLLHYQKKGQWYEIYDKHQVIQTLDCILYWKVLQKKVGKIHIVEKQKMTEEVLEFQKQLNYLIGY 160
Cdd:pfam19710   84 TNLCPDFYQKFSPDQFILLYQKKGQWYEIYDKHQVFQTLDCIRYWKALQKDVGKIHLVQRPQPSEESLQYQRQLNYLIGY 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1716990059  161 DVTDVSNVHDDELEFTRRRLVTPRVIELASRD 192
Cdd:pfam19710  164 DVTDVSNVHDDELEFTRRKLVTPRMIELSDRD 195
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 737-1094 3.08e-112

Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kbeta can be activated by G-protein-coupled receptors. Deletion of PI3Kbeta in mice results in early lethality at around day three of development. PI3Kbeta plays an important role in regulating sustained integrin activation and stable platelet agrregation, especially under conditions of high shear stress. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270717 [Multi-domain]  Cd Length: 362  Bit Score: 353.11  E-value: 3.08e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  737 KQVQVTEMLHKVTMEIK--SISAEKYDVTSQVITQLRQKLDKMQSSNFpesfRVPYDPGLRAGTLVVEKCKVMASKKKPL 814
Cdd:cd05173      6 KQVEALNKLKTLNSLIKlnAVKLSKAKGKEAMHTCLRQSAYREALSDL----QSPLNPSIILSELNVEKCKYMDSKMKPL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  815 WLEFkcaDPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIAKI 894
Cdd:cd05173     82 WIVY---NNKLFGGDSLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAETIADI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  895 Q--QSTVGNTGAFKDEVLNQWLKEkCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHIL 972
Cdd:cd05173    159 QlnSSNVAAAAAFNKDALLNWLKE-YNSGDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHIL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  973 GNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIE 1052
Cdd:cd05173    238 GNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAGLPELTSVKDIQ 317

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1716990059 1053 YIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLV 1094
Cdd:cd05173    318 YLKDSLALGKSEEEALKQFRQKFDEALRESWTTKVNWMAHTV 359
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 732-1094 3.38e-112

Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kdelta is mainly expressed in immune cells and plays an important role in cellular and humoral immunity. It plays a major role in antigen receptor signaling in B-cells, T-cells, and mast cells. It regulates the differentiation of peripheral helper T-cells and controls the development and function of regulatory T-cells. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270718 [Multi-domain]  Cd Length: 366  Bit Score: 353.20  E-value: 3.38e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  732 LHDFMK-------QVQVTEMLHKVtmeiksISAEKYdvtsqvitqlRQKLDKMQSsnfpesfrvPYDPGLRAGTLVVEKC 804
Cdd:cd05174     20 LNDFVKvssqkatKPQTKEMMHVC------MKQETY----------MEALSHLQS---------PLDPSIILEEVCVDQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  805 KVMASKKKPLWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEI 884
Cdd:cd05174     75 TFMDSKMKPLWIMYSSEEAGA---GNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLSTGDKTGLIEV 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  885 VKDATTIAKIQ--QSTVGNTGAFKDEVLNQWLKEKCPvEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGN 962
Cdd:cd05174    152 VLHSDTIANIQlnKSNMAATAAFNKDALLNWLKSKNP-GDALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQ 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  963 LFHIDFGHILGNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGM 1042
Cdd:cd05174    231 LFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMKAAGL 310

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1716990059 1043 PQLTSKEDIEYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLV 1094
Cdd:cd05174    311 PELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNV 362
C2_PI3K_class_I_gamma cd08399
C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 350-530 1.38e-110

C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, gamma isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176044  Cd Length: 178  Bit Score: 341.51  E-value: 1.38e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  350 FTISLWDCNRKFRVKVIGIDIPVLPRNTELMVFVEANIQHGQQLLAQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALL 429
Cdd:cd08399      1 FTVSLWDCDRKFRVKILGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNTWLEFDIKIKDLPKGALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  430 NLQIYCGKSPSLTTKTNVQphdTLSSDSKCKNQLLYYVNLLLIDHRFLLRQGDYVLHMWKIPGKGEEQGSINADKLTSAT 509
Cdd:cd08399     81 NLQIYCGKAPALSSKKSAE---SPSSESKGKHQLLYYVNLLLIDHRFLLRTGEYVLHMWQISGKGEDQGSVNADKLTSAT 157

                          170       180
                   ....*....|....*....|.
gi 1716990059  510 NPDKETSMAISIVLDRYCHPI 530
Cdd:cd08399    158 NPDKENSMSISILLDNYCHPV 178
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 727-1094 6.91e-98

Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kalpha plays an important role in insulin signaling. It also mediates physiologic heart growth and provides protection from stress. Activating mutations of PI3Kalpha is associated with diverse forms of cancer at high frequency. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270719 [Multi-domain]  Cd Length: 370  Bit Score: 315.07  E-value: 6.91e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  727 CGKAMLHdFMKQVQVTEMLHKVTMEIKSisaEKYDVTSQVitQLRQKLDKMQSSNFPES---FRVPYDPGLRAGTLVVEK 803
Cdd:cd05175      1 CGMYLKH-LSRQVEAMEKLINLTDILKQ---EKKDETQKV--QMKFLVEQMRRPDFMDAlqgFLSPLNPAHQLGNLRLEE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  804 CKVMASKKKPLWLEFKCAD-PTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMI 882
Cdd:cd05175     75 CRIMSSAKRPLWLNWENPDiMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  883 EIVKDATTIAKIQQSTvGNTGA--FKDEVLNQWLKEKCPvEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITES 960
Cdd:cd05175    155 EVVRNSHTIMQIQCKG-GLKGAlqFNSHTLHQWLKDKNK-GEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDD 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  961 GNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLYVMGTSGKKTSQ--HFHKFEDVCVKAYLALRHHTNLLIILFSMML 1038
Cdd:cd05175    233 GQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKtrEFERFQEMCYKAYLAIRQHANLFINLFSMML 312

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1716990059 1039 MTGMPQLTSKEDIEYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLV 1094
Cdd:cd05175    313 GSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTI 368
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 734-1092 9.31e-91

Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270720 [Multi-domain]  Cd Length: 353  Bit Score: 295.35  E-value: 9.31e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  734 DFMKQVQVTEMLHKVTMEIKSISAEKYDVTsqvitqLRQKLDKMQSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKKKP 813
Cdd:cd05176      3 ELEKQTRLVQLLGRVAEKVRQASGSARQVA------LQDGMERVQSFFQKNKCRLPLSPSLVAKELNIKACSFFSSNAVP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  814 LWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIAK 893
Cdd:cd05176     77 LKVALVNADPLG---EEINVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPSSDTLRK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  894 IQQStVGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHILG 973
Cdd:cd05176    154 IQVE-YGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLG 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  974 NYKSFLGINKERVPFVLTPDFLYVMgTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEY 1053
Cdd:cd05176    233 HAQMFGSFKRDRAPFVLTSDMAYVI-NGGEKPTIRFQLFVDLCCQAYNLIRKHTNLFLNLLSLMLSSGLPELTGIQDLKY 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1716990059 1054 IRDALTVGRSEDEAKRHFLDQIEICRDKGWTvQFNWFLH 1092
Cdd:cd05176    312 VFDALQPQTTDAEATIFFTRLIESSLGSVAT-KFNFFIH 349
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 734-1076 2.46e-86

Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II gamma isoform, PI3K-C2gamma, is expressed in the liver, breast, and prostate. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. It's biological function remains unknown. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270721 [Multi-domain]  Cd Length: 354  Bit Score: 283.32  E-value: 2.46e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  734 DFMKQVQVTEMLHKVTMEIKSISAEKydvtsqvitqlRQKLDKMQSSNFPESF------RVPYDPGLRAGTLVVEKCKVM 807
Cdd:cd05177      3 EFSKETKLISILIDAAEKVKTASDTR-----------RKEVLKREASRLEDFFqdvvscCLPLNPALRVKGIDADACSYF 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  808 ASKKKPLWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKD 887
Cdd:cd05177     72 TSNAAPLKISFINANPLA---KNISIIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGLVQMVPD 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  888 ATTIAKIQQSTvGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHID 967
Cdd:cd05177    149 AVTLAKIHRES-GLIGPLKENTIEKWFHMHNKLKEDYDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSGHMFHID 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  968 FGHILGNYKSFLGINKERVPFVLTPDFLYVMgTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTS 1047
Cdd:cd05177    228 FGKFLGHAQTFGSIKRDRAPFIFTSEMEYFI-TEGGKKPQRFQRFVELCCRAYNIVRKHSQLLLNLLEMMLHAGLPELKD 306

                          330       340
                   ....*....|....*....|....*....
gi 1716990059 1048 KEDIEYIRDALTVGRSEDEAKRHFLDQIE 1076
Cdd:cd05177    307 IQDLKYVYNNLRPQDTDLEATSYFTKKIK 335
PI3Ka_I cd00872
Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all ...
 552-728 8.04e-86

Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3K class I prefer phosphoinositol (4,5)-bisphosphate as a substrate. Mammalian members interact with active Ras. They form heterodimers with adapter molecules linking them to different signaling pathways.


Pssm-ID: 238444  Cd Length: 171  Bit Score: 274.58  E-value: 8.04e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  552 NQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAkkeawDRSSLDVGLTM 631
Cdd:cd00872      1 NEEREQLEAIIARDPLSELTEEDKELLWKLRHECRKKPQALPKLLLSVKWNKRDDVAQMYQLLK-----RWPKLKPEQAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  632 QLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIAQSMH 711
Cdd:cd00872     76 ELLDCNFPDEHVREFAVRCLEKLSDDELLQYLLQLVQVLKYEPYHDSDLVRFLLKRALRNQRIGHFFFWHLRSEMHNPSV 155

                          170
                   ....*....|....*..
gi 1716990059  712 yQQRFAVLLEAYLRGCG 728
Cdd:cd00872    156 -SQRFGLLLEAYLRGCG 171
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 734-1092 5.31e-84

Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 119421 [Multi-domain]  Cd Length: 354  Bit Score: 276.88  E-value: 5.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  734 DFMKQVQVTEMLHKVTMEIKSISAEkydvTSQVItqLRQKLDKM-QSSNFPESFRVPYDPGLRAGTLVVEKCKVMASKKK 812
Cdd:cd00895      3 EFDRQCWLVNVLAKLAQQVREAAPS----ARQGI--LREGLEEVkQFFSINGSCRLPLSPSLLVKGIVPRDCSYFNSNAV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  813 PLWLEFKCADPTAlsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIA 892
Cdd:cd00895     77 PLKLSFQNVDPLG---ENIRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLR 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  893 KIQQSTvGNTGAFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHIL 972
Cdd:cd00895    154 KIQVEH-GVTGSFKDRPLADWLQKHNPTEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  973 GNYKSFLGINKERVPFVLTPDFLYVMgTSGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIE 1052
Cdd:cd00895    233 GHAQMFGNIKRDRAPFVFTSDMAYVI-NGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLK 311

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1716990059 1053 YIRDALTVGRSEDEAKRHFLDQIEICRDKGWTvQFNWFLH 1092
Cdd:cd00895    312 YVYDALRPQDTEADATTYFTRLIESSLGSVAT-KLNFFIH 350
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 833-1049 4.26e-79

Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in a variety of processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced, the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 259.15  E-value: 4.26e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   833 IIFKHGDDLRQDMLILQILRIMESIWEAEA----LDLCLLPYGCISTGNKIGMIEIVKDATTIAKIQ------------- 895
Cdd:smart00146    1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDKetrrRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILkeyrkqkgkvldl 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   896 -----------QSTVGNTGAFKDEVLNQWLKEKCPVE-EKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNL 963
Cdd:smart00146   81 rsqtatrlkklELFLEATGKFPDPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGHL 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   964 FHIDFGHILGNYKSFLGiNKERVPFVLTPDFLYVMGTSGkktsqHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMP 1043
Cdd:smart00146  161 FHIDFGFILGNGPKLFG-FPERVPFRLTPEMVDVMGDSG-----YFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLP 234


                    ....*.
gi 1716990059  1044 QLTSKE 1049
Cdd:smart00146  235 DWRSGK 240
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 729-1076 2.67e-77

Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class III PI3Ks, also called Vps34 (vacuolar protein sorting 34), contain an N-terminal lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They phosphorylate only the substrate PtdIns. They interact with a regulatory subunit, Vps15, to form a membrane-associated complex. Class III PI3Ks are involved in protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270628 [Multi-domain]  Cd Length: 346  Bit Score: 258.23  E-value: 2.67e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  729 KAMLHdfmKQVQVTEMLHKVTMEIKSISAEKydvtSQVITQLRQKLDKMQSSN--FPESFRVPYDPGLRAGTLVVEKCKV 806
Cdd:cd00896      1 REALK---RQQEFVDRLRSLMKEVKNEKGSR----DKKIERLRELLSDSELGLllFFEPLPLPLDPSVKVTGIIPEKSTV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  807 MASKKKPLWLEFKCADPtalsnETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVK 886
Cdd:cd00896     74 FKSALMPLKLTFKTLDG-----GEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  887 DATTIAKIQQstvgntgafKDEVLNQWLK-----EKCPVEEKFCAsVERFVYSCAGYCVATYVLGIGDRHNDNIMITESG 961
Cdd:cd00896    149 NSKALADILK---------KYGSILNFLRkhnpdESGPYGIKPEV-MDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDG 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  962 NLFHIDFGHILGN-YKSFLginkerVPFVLTPDFLYVMGtsGKKtSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMT 1040
Cdd:cd00896    219 HLFHIDFGYILGRdPKPFP------PPMKLCKEMVEAMG--GAN-SEGYKEFKKYCCTAYNILRKHANLILNLFSLMVDA 289

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1716990059 1041 GMP--QLTSKEDIEYIRDALTVGRSEDEAKRHFLDQIE 1076
Cdd:cd00896    290 NIPdiALEPDKAVLKVQEKFRLDLSDEEAEQYFQNLID 327
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 797-1040 7.14e-77

Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family include PI3K, phosphoinositide 4-kinase (PI4K), PI3K-related protein kinases (PIKKs), and TRansformation/tRanscription domain-Associated Protein (TRAPP). PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives, while PI4K catalyze the phosphorylation of the 4-hydroxyl of PtdIns. PIKKs are protein kinases that catalyze the phosphorylation of serine/threonine residues, especially those that are followed by a glutamine. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI4Ks produce PtdIns(4)P, the major precursor to important signaling phosphoinositides. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PI3K-like catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270621 [Multi-domain]  Cd Length: 216  Bit Score: 251.87  E-value: 7.14e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  797 GTLVVEKCKVMASKKKPLWLEFKCADptalsNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTG 876
Cdd:cd00142      1 NALDVGILKVIHSKQRPKKITLIGAD-----GKTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYKVIPLS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  877 NKIGMIEIVKDATTIakiqqstvgntgafkdEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIM 956
Cdd:cd00142     76 ENSGLIEIVKDAQTI----------------EDLLKSLWRKSPSSQSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIM 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  957 ITESGNLFHIDFGHILGNYKSFLGinKERVPFVLTPDFLYVMGTSGkktsqHFHKFEDVCVKAYLALRHHTNLLIILFSM 1036
Cdd:cd00142    140 IEPSGNIFHIDFGFIFSGRKLAEG--VETVPFRLTPMLENAMGTAG-----VNGPFQISMVKIMEILREHADLIVPILEH 212


                   ....
gi 1716990059 1037 MLMT 1040
Cdd:cd00142    213 SLRD 216
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 547-735 1.87e-74

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 395488  Cd Length: 185  Bit Score: 243.78  E-value: 1.87e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  547 RTEMPNQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAKkeaWDRssLD 626
Cdd:pfam00613    2 DLKPNEKERKELEAILAYDPLSKLTAEEKDLIWKFRYYLMLVPKALTKLLLSVKWSDLSEVAEALSLLLK---WAP--ID 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  627 VGLTMQLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEI 706
Cdd:pfam00613   77 PVDALELLDPKFPDPEVRQYAVKCLESASDDELLFYLLQLVQALKYEPFHDSYLSRFLLQRALKNRRIGHFFFWYLKSEI 156

                          170       180
                   ....*....|....*....|....*....
gi 1716990059  707 AQSmHYQQRFAVLLEAYLRGCGKAMLHDF 735
Cdd:pfam00613  157 HDE-EVSPRFGSLLELYLRSCGTSLLGLN 184
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 551-735 1.15e-72

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 214537  Cd Length: 184  Bit Score: 239.08  E-value: 1.15e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   551 PNQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIK-HPKAYPKLLASVKWGHQETVAKTYQLLAKkeaWDrsSLDVGL 629
Cdd:smart00145    4 DIEEREQLEAILKLDPTYELTEEEKDLIWKFRHYYLTnNPKALPKFLLSVKWSDADEVAQALSLLLS---WA--PLDPED 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   630 TMQLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIaQS 709
Cdd:smart00145   79 ALELLDPKFPDPFVRAYAVKRLESASDEELLLYLLQLVQALKYEPYLDSALARFLLERALANQRLGHFFYWYLKSEL-HD 157

                           170       180
                    ....*....|....*....|....*.
gi 1716990059   710 MHYQQRFAVLLEAYLRGCGKAMLHDF 735
Cdd:smart00145  158 PHVSIRFGLLLEAYLRGCGTHLKELL 183
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 831-1047 1.00e-70

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 235.69  E-value: 1.00e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  831 IGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLL-PYGCISTGNKIGMIEIVKDATTIAKIQQ----STVGNTGAF 905
Cdd:pfam00454    2 YGGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRRLkPYSVIPLGPKCGIIEWVPNSETLAYILDeygeNGVPPTAMV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  906 KD-----------------------EVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMI-TESG 961
Cdd:pfam00454   82 KIlhsalnypklklefesrislppkVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVdKTTG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  962 NLFHIDFGHILGNYKSFLGINkERVPFVLTPDFLYVMGTSGkktsqHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTG 1041
Cdd:pfam00454  162 KLFHIDFGLCLPDAGKDLPFP-EKVPFRLTREMVYAMGPSG-----DEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235


                   ....*.
gi 1716990059 1042 MPQLTS 1047
Cdd:pfam00454  236 LPDWSI 241
PI3Ka cd00864
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 552-706 2.42e-60

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in PI3 and PI4-kinases. Its role is unclear, but it has been suggested to be involved in substrate presentation. Phosphoinositide 3-kinases play an important role in a variety of fundamental cellular processes and can be divided into three main classes, defined by their substrate specificity and domain architecture.


Pssm-ID: 238440  Cd Length: 152  Bit Score: 203.22  E-value: 2.42e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  552 NQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAKKEAwdrssLDVGLTM 631
Cdd:cd00864      1 AWERKPLLAILLYPPFSTLTEEEKELLWKFRYYLLNVPKALPKLLKSVNWNDDEEVSELYQLLKWWAP-----LSPEDAL 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716990059  632 QLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEI 706
Cdd:cd00864     76 ELLSPKYPDPVVRQYAVRVLESASDDELLLYLPQLVQALKYEPYLDSYLARFLLERALKSQRLGHQLYWNLKSEI 150
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 802-1098 1.72e-57

Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIalpha is a 220 kDa protein found in the plasma membrane and the endoplasmic reticulum (ER). The role of PI4KIIIalpha in the ER remains unclear. In the plasma membrane, it provides PtdIns(4)P, which is then converted by PI5Ks to PtdIns(4,5)P2, an important signaling molecule. Vertebrate PI4KIIIalpha is also part of a signaling complex associated with P2X7 ion channels. The yeast homolog, Stt4p, is also important in regulating the conversion of phosphatidylserine to phosphatidylethanolamine at the ER and Golgi interface. Mammalian PI4KIIIalpha is highly expressed in the nervous system. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270711 [Multi-domain]  Cd Length: 307  Bit Score: 200.90  E-value: 1.72e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  802 EKCKVMASKKK-PLWLEFKCADPTALSNETIGI------------IFKHGDDLRQDMLILQILRIMESIWEAEALDLCLL 868
Cdd:cd05167      8 KSGKPLQSAAKaPFLVTFKVKDCGVDELEHEGTeseatkevwqaaIFKVGDDCRQDMLALQLISLFKNIFEEVGLDLYLF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  869 PYGCISTGNKIGMIEIVKDATTIAKIQQSTVGNtgafkdevLNQWLKEKCPVEE--KFCASVERFVYSCAGYCVATYVLG 946
Cdd:cd05167     88 PYRVVATGPGCGVIEVIPNSKSRDQIGRETDNG--------LYEYFLSKYGDEStpAFQKARRNFIKSMAGYSLVSYLLQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  947 IGDRHNDNIMITESGNLFHIDFGHIL-----GNyksflgINKERVPFVLTPDFLYVMGtsGKKTSQHFHKFEDVCVKAYL 1021
Cdd:cd05167    160 IKDRHNGNIMIDDDGHIIHIDFGFIFeispgGN------LGFESAPFKLTKEMVDLMG--GSMESEPFKWFVELCVRGYL 231

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1716990059 1022 ALRHHTNLLIILFSMMLMTGMPQLTsKEDIEYIRDALTVGRSEDEAKRHFLDQIEICRDKGWTVQFNWFLHLVLGIK 1098
Cdd:cd05167    232 AVRPYAEAIVSLVELMLDSGLPCFR-GQTIKNLRERFALEMSEREAANFMIKLIADSYLKIRTKGYDMFQYYQNGIP 307
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 833-1097 6.63e-54

Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. There are two types of PI4Ks, types II and III. Type II PI4Ks lack the characteristic catalytic kinase domain present in PI3Ks and type III PI4Ks, and are excluded from this family. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270626 [Multi-domain]  Cd Length: 286  Bit Score: 189.78  E-value: 6.63e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  833 IIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIAKIQQSTvGNTGAFKDevLNQ 912
Cdd:cd00893     30 LIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEILSLGPDSGIIEMIKNAVSIDSLKKKL-DSFNKFVS--LSD 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  913 WLKEKCPvEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHILGNYKSFLGInkERVPFVLTP 992
Cdd:cd00893    107 FFDDNFG-DEAIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDKEGHIIHIDFGFFLSSHPGFYGF--EGAPFKLSS 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  993 DFLYVMgtsGKKTSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGRSEDEAKRHFL 1072
Cdd:cd00893    184 EYIEVL---GGVDSELFKEFRKLFLKGFMALRKHSDKILSLVEMMYSGHGITCFGKKTIQQLKQRFNPELTEGELEVYVL 260

                          250       260
                   ....*....|....*....|....*
gi 1716990059 1073 DQIEICRDKGWTVQFNWFLHLVLGI 1097
Cdd:cd00893    261 SLINKSLDNWRTRWYDKYQYFSQGI 285
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 831-1097 1.52e-51

Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIbeta (also called Pik1p in yeast) is a 110 kDa protein that is localized to the Golgi and the nucleus. It is required for maintaining the structural integrity of the Golgi complex (GC), and is a key regulator of protein transport from the GC to the plasma membrane. PI4KIIIbeta also functions in the genesis, transport, and exocytosis of synaptic vesicles. The Drosophila PI4KIIIbeta is essential for cytokinesis during spermatogenesis. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 183.45  E-value: 1.52e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  831 IGIIFKHGDDLRQDMLILQILRIMESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTIAKIQQSTVGNTGafkdevL 910
Cdd:cd05168     31 RSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSGLIETIPDTVSIDSLKKRFPNFTS------L 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  911 NQWLKEKC--PVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMITESGNLFHIDFGHILGNYKSflGINKERVPF 988
Cdd:cd05168    105 LDYFERTFgdPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHIIHIDFGFMLSNSPG--GLGFETAPF 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  989 VLTPDFLYVMGtsGKKtSQHFHKFEDVCVKAYLALRHHTNLLIILFSMMLMTG-MPQLT--SKEDIEYIRDALTVGRSED 1065
Cdd:cd05168    183 KLTQEYVEVMG--GLE-SDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSkLPCFFggGEFTIEQLRERFKLNLTEE 259

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1716990059 1066 EAKRHFLDQIEICRDKGWTVQFNWFLHLVLGI 1097
Cdd:cd05168    260 ECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGI 291
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
809-1076 2.09e-40

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 163.42  E-value: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  809 SKKKPLWLEFKCADptalsNETIGIIFKHGDDLRQDMLILQILRIMESIW----EAEALDLCLLPYGCISTGNKIGMIEI 884
Cdd:COG5032   1780 HLQRPRRLTIRGSD-----GKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEW 1854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  885 VKDATTIAKI------------------QQSTVGNTGAFKDE-----------VLNQWLKEKCPVEEKFCASVERFVYSC 935
Cdd:COG5032   1855 VPNSDTLHSIlreyhkrknisidqekklAARLDNLKLLLKDEfftkatlksppVLYDWFSESFPNPEDWLTARTNFARSL 1934

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  936 AGYCVATYVLGIGDRHNDNIMITE-SGNLFHIDFGHILGNYKSFLGINkERVPFVLTPDFLYVMGTSGKKTSqhfhkFED 1014
Cdd:COG5032   1935 AVYSVIGYILGLGDRHPGNILIDRsSGHVIHIDFGFILFNAPGRFPFP-EKVPFRLTRNIVEAMGVSGVEGS-----FRE 2008

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1716990059 1015 VCVKAYLALRHHTNLLIILFSMML------------MTGMPQLTSKEDIEYIRDALTvgrsEDEAKRHFLDQIE 1076
Cdd:COG5032   2009 LCETAFRALRKNADSLMNVLELFVrdpliewrrlpcFREIQNNEIVNVLERFRLKLS----EKDAEKFVDLLIN 2078
PI3Ka_II cd00869
Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is ...
 556-722 2.66e-35

Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, class II PI3-kinases phosphorylate phosphoinositol (PtdIns), PtdIns(4)-phosphate, but not PtdIns(4,5)-bisphosphate. They are larger, having a C2 domain at the C-terminus.


Pssm-ID: 238441  Cd Length: 169  Bit Score: 132.20  E-value: 2.66e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  556 KQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLakkEAWdrSSLDVGLTMQLLD 635
Cdd:cd00869      5 EKLLDLIQKQSTYTLSTEDKDLLWEKRLYCTNEPNALPLVLASAPSWDWANLMDVYQLL---HQW--APLRPLIALELLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  636 CNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYHDSALAKFLLKRALRSKRIGHFLFWFLRSEIAQSmHYQQR 715
Cdd:cd00869     80 PKFPDQEVRAHAVQWLARLSNDELLDYLPQLVQALKFELYLKSALVRFLLSRSLVSLRFAHELYWLLKDALDDC-YFSSA 158


                   ....*..
gi 1716990059  716 FAVLLEA 722
Cdd:cd00869    159 YQDLGAA 165
PI3Ka_III cd00870
Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is ...
 551-706 2.95e-34

Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3Ks class III phosphorylate phosphoinositol (PtdIns) only. The prototypical PI3K class III, yeast Vps34, is involved in trafficking proteins from Golgi to the vacuole.


Pssm-ID: 238442  Cd Length: 166  Bit Score: 128.99  E-value: 2.95e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  551 PNQLRKQLEEIIATDPLNPLTPEDKELLWHFRYESIKHPKAYPKLLASVKWGHQETVAKTYQLLAKkeaWdrSSLDVGLT 630
Cdd:cd00870      7 NSKERKELNKILKYPPTTKLTDEEKDLIWKFRFYLTNNKKALTKFLKSVNWSDEQEVKQALELMPK---W--AKIDIEDA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  631 MQLLDCNFPDENVRAMAVQKLESLQDDDVLHYLLQLVQAVKFEPYH-------DSALAKFLLKRALRSKRIGHFLFWFLR 703
Cdd:cd00870     82 LELLSPYFTNPVVRKYAVSRLKLASDEELLLYLLQLVQALKYENLDlsplprlDSPLADFLIERALKNPKLANFLYWYLK 161


                   ...
gi 1716990059  704 SEI 706
Cdd:cd00870    162 VEL 164
C2_PI3K_like cd08380
C2 domain present in phosphatidylinositol 3-kinases (PI3Ks); C2 domain present in all classes ...
 352-530 3.86e-34

C2 domain present in phosphatidylinositol 3-kinases (PI3Ks); C2 domain present in all classes of PI3Ks. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains members with the first C2 repeat, C2A, and a type-I topology, as well as some with a single C2 repeat.


Pssm-ID: 176026  Cd Length: 156  Bit Score: 128.25  E-value: 3.86e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  352 ISLWDCNRKFRVKVIGIDIPVLPRNTELMVFVEANIQHGQQLLAQRRTT-CKPFTEEVLWNTWLDFDIKIKDLPKGALLN 430
Cdd:cd08380      1 KSLWDINFNLRIKIHGITNINLLDSEDLKLYVRVQLYHGGEPLCPPQSTkKVPFSTSVTWNEWLTFDILISDLPREARLC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  431 LQIYCGKSPSLTtktnvqphdtlssdskcKNQLLYYVNLLLIDHRFLLRQGDYVLHMWKIPGKGEEQGsinadklTSATN 510
Cdd:cd08380     81 LSIYAVSEPGSK-----------------KEVPLGWVNVPLFDYKGKLRQGMITLNLWPGKKTDPRIA-------CTPCN 136

                          170       180
                   ....*....|....*....|
gi 1716990059  511 PDKETSMAISIVLDRYCHPI 530
Cdd:cd08380    137 NSNENSTRLLIELPEFSKPV 156
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 805-1038 5.04e-28

Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members include ATM (Ataxia telangiectasia mutated), ATR (Ataxia telangiectasia and Rad3-related), TOR (Target of rapamycin), SMG-1 (Suppressor of morphogenetic effect on genitalia-1), and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP, ATM and TRRAP, C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270708 [Multi-domain]  Cd Length: 222  Bit Score: 113.14  E-value: 5.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  805 KVMASKKKPLWLEFKCadptalSNETIGI-IFKHGDDLRQDMLILQILRIMESIWEAEA----LDLCLLPYGCISTGNKI 879
Cdd:cd05164      9 RILASLQKPKKITILG------SDGKEYPfLVKGDDDLRKDERVMQLFQLLNTLLEKDKetrkRNLTIRTYSVVPLSSQS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  880 GMIEIVKDATTiakiqqstvgntgaFKDeVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMI-T 958
Cdd:cd05164     83 GLIEWVDNTTT--------------LKP-VLKKWFNETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIdT 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  959 ESGNLFHIDFGHILGNYKSFLgiNKERVPFVLTPDFLYVMGTSGKKTsqhfhKFEDVCVKAYLALRHHTNLLIILFSMML 1038
Cdd:cd05164    148 KTGEVVHIDFGMIFNKGKTLP--VPEIVPFRLTRNIINGMGPTGVEG-----LFRKSCEQVLRVFRKHKDKLITFLDTFL 220
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 806-999 2.75e-26

Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, containing the Ku70/80 subunit, and a catalytic subunit, which contains a NUC194 domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is part of a multi-component system involved in non-homologous end joining (NHEJ), a process of repairing double strand breaks (DSBs) by joining together two free DNA ends of little homology. DNA-PK functions as a molecular sensor for DNA damage that enhances the signal via phosphorylation of downstream targets. It may also act as a protein scaffold that aids the localization of DNA repair proteins to the site of DNA damage. DNA-PK also plays a role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. DNA-PK is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The DNA-PK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270716 [Multi-domain]  Cd Length: 235  Bit Score: 108.43  E-value: 2.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  806 VMASKKKPLWLEFKCADptalsNETIGIIFKHGDDLRQDMLILQILRIMESIWEAEA----LDLCLLPYGCISTGNKIGM 881
Cdd:cd05172     10 VLSSKRRPKRITIRGSD-----EKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPacrqRRLRIRTYQVIPMTSRLGL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  882 IEIVKDATTIAKIqqstvgntgaFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMI-TES 960
Cdd:cd05172     85 IEWVDNTTPLKEI----------LENDLLRRALLSLASSPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVdLST 154

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1716990059  961 GNLFHIDFGHILGNYKSFLGInKERVPFVLTPDFLYVMG 999
Cdd:cd05172    155 GRLIGIDFGHAFGSATQFLPI-PELVPFRLTRQLLNLLQ 192
PI3K_rbd smart00144
PI3-kinase family, Ras-binding domain; Certain members of the PI3K family possess Ras-binding ...
 203-312 1.13e-25

PI3-kinase family, Ras-binding domain; Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding RA domains (unpublished observation).


Pssm-ID: 197540  Cd Length: 108  Bit Score: 102.41  E-value: 1.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   203 TSKPLPEYMFKKITSSNVFIVIHR--GTTSQTIKVSIDDTPNMILQTFFTKiakKKSLLDiPEDHSELDFVLRVCGRDEY 280
Cdd:smart00144    1 TSPSVPEPLPLKTIANKILIVVHLekDQQTKTLKVNPNCTPDSVLAQAFTK---MLSLHD-QVDPTSEDYILKVCGRDEY 76

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1716990059   281 IIGDTPIRDFHWIRECHKNGEEIHLVLDTPPD 312
Cdd:smart00144   77 LLGDHPLGSFEYIRNCLKNGTEPHLVLMTLSA 108
PI3K_C2 smart00142
Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.
 349-444 3.74e-23

Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.


Pssm-ID: 214536  Cd Length: 100  Bit Score: 95.11  E-value: 3.74e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059   349 VFTISLWDCNRKFRVKVIGIDIPVLPRNTELM-VFVEANIQHGQQLL-AQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKG 426
Cdd:smart00142    1 VKIESLWDCDRNLVITIALIHGIPLNWSRDYSdLYVEIQLYHGGKLLcLPVSTSYKPFFPSVKWNEWLTFPIQISDLPRE 80

                            90
                    ....*....|....*...
gi 1716990059   427 ALLNLQIYCGKSPSLTTK 444
Cdd:smart00142   81 ARLCITIYAVKNPSKGSE 98
PI3K_rbd pfam00794
PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding ...
 203-312 5.62e-23

PI3-kinase family, ras-binding domain; Certain members of the PI3K family possess Ras-binding domains in their N-termini. These regions show some similarity (although not highly significant similarity) to Ras-binding pfam00788 domains (unpublished observation).


Pssm-ID: 395642  Cd Length: 106  Bit Score: 94.67  E-value: 5.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  203 TSKPLPEYMfKKITSSNVFIVIH--RGTTSQTIKVSIDDTPNMILQTFFTKiakKKSLLDIPEdhSELDFVLRVCGRDEY 280
Cdd:pfam00794    1 ASTVSPEPL-PKLINNKLLISVHleGDQMTKTFTCNPNSTPGSLIAQALTK---KLSVHTQGD--VTDDYVLKVCGRDEY 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1716990059  281 IIGDTPIRDFHWIRECHKNGEEIHLVLDTPPD 312
Cdd:pfam00794   75 LLGDHPLGQFEYIRNCLKSGREPHLTLVEQSS 106
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 811-969 4.19e-20

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 87.50  E-value: 4.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  811 KKPLWLEFKCadptalsnETIGIIFKHGDD--------LRQDMLILQILRIMEsiweaealdlcLLPYGCIST----GNK 878
Cdd:cd13968      7 AKVFWAEGEC--------TTIGVAVKIGDDvnneegedLESEMDILRRLKGLE-----------LNIPKVLVTedvdGPN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  879 IGMIEIVKDATTIAKIQQstvgntgafkdevlnqwlkekcpvEEKFCASVERFVYSCAGYCVATYV--LGIGDRHNDNIM 956
Cdd:cd13968     68 ILLMELVKGGTLIAYTQE------------------------EELDEKDVESIMYQLAECMRLLHSfhLIHRDLNNDNIL 123

                          170
                   ....*....|...
gi 1716990059  957 ITESGNLFHIDFG 969
Cdd:cd13968    124 LSEDGNVKLIDFG 136
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 802-1037 3.06e-19

Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to as Mei-41 (Drosophila), Esr1/Mec1p (Saccharomyces cerevisiae), Rad3 (Schizosaccharomyces pombe), and FRAP-related protein (human). ATR contains a UME domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. Together with its downstream effector kinase, Chk1, ATR plays a central role in regulating the replication checkpoint. ATR stabilizes replication forks by promoting the association of DNA polymerases with the fork. Preventing fork collapse is essential in preserving genomic integrity. ATR also plays a role in normal cell growth and in response to DNA damage. ATR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 87.95  E-value: 3.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  802 EKCKVMASKKKPLWLEFKCADptalsNETIGIIFKHGDDLRQDM----LILQILRIMESIWEAEALDLCLLPYGCISTGN 877
Cdd:cd00892      6 DEVEIMPSLQKPKKITLVGSD-----GKKYPFLCKPKDDLRKDArmmeFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  878 KIGMIEIVKDATTIAKIQQStvgntgaFKDEVLNQWLKEKCPVEEKFCASVERFVYSCAGYCVATYVLGIGDRHNDNIMI 957
Cdd:cd00892     81 ECGIIEWVPNTVTLRSILST-------LYPPVLHEWFLKNFPDPTAWYEARNNYTRSTAVMSMVGYILGLGDRHGENILF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  958 -TESGNLFHIDFGHILGNYKSfLGInKERVPFVLTPDFLYVMGTSGKKTSqhfhkFEDVCVKAYLALRHHTNLLI-ILFS 1035
Cdd:cd00892    154 dSTTGDVVHVDFDCLFDKGLT-LEV-PERVPFRLTQNMVDAMGVTGVEGT-----FRRTCEVTLRVLRENRETLMsVLET 226


                   ..
gi 1716990059 1036 MM 1037
Cdd:cd00892    227 FV 228
C2_PI3K_class_I_beta_delta cd08693
C2 domain present in class I beta and delta phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 352-526 1.54e-17

C2 domain present in class I beta and delta phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, beta and delta isoforms of PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176075  Cd Length: 173  Bit Score: 81.20  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  352 ISLWDCNRKFRVKVIGI-DIPVLPRNteLMVFVEANIQHGQQLL-AQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALL 429
Cdd:cd08693      1 KSLWDIEEKFSITLHKIsNLNAAERT--MKVGVQAGLFHGGESLcKTVKTSEVSGKNDPVWNETLEFDINVCDLPRMARL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  430 NLQIY-CGKSPSLTTKTNVQphdtlssdSKCKNQLLYY----VNLLLIDHRFLLRQGDYVLHMWKIPgkgEEQGSINADK 504
Cdd:cd08693     79 CFAIYeVSKKAKGKRSRKNQ--------TKKKKKKDDNpiawVNTMVFDYKGQLKTGDHTLYMWTYA---EDQSEDLLNP 147

                          170       180
                   ....*....|....*....|...
gi 1716990059  505 L-TSATNPDKETSMAISIVLDRY 526
Cdd:cd08693    148 LgTVESNPNTESATALHISFPEY 170
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 834-1002 1.67e-15

Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA double strand breaks (DSBs) caused by radiation. It is activated at the site of a DSB and phosphorylates key substrates that trigger pathways that regulate DNA repair and cell cycle checkpoints at the G1/S, S phase, and G2/M transition. Patients with the human genetic disorder Ataxia telangiectasia (A-T), caused by truncating mutations in ATM, show genome instability, increased cancer risk, immunodeficiency, compromised mobility, and neurodegeneration. A-T displays clinical heterogeneity, which is correlated to the degree of retained ATM activity. ATM contains a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATM catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270715 [Multi-domain]  Cd Length: 282  Bit Score: 78.35  E-value: 1.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  834 IFKHGDDLRQDMLILQILRIMESIW----EAEALDLCLLPYGCISTGNKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEV 909
Cdd:cd05171     33 LVKGGDDLRQDAVMEQVFELVNQLLkrdkETRKRKLRIRTYKVVPLSPRSGVLEFVENTIPLGEYLVGASSKSGAHARYR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  910 LNQWLKEKC----------PVEEKF------CASV---------ERFV-----------Y--SCAGYCVATYVLGIGDRH 951
Cdd:cd05171    113 PKDWTASTCrkkmrekakaSAEERLkvfdeiCKNFkpvfrhfflEKFPdpsdwferrlaYtrSVATSSIVGYILGLGDRH 192

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1716990059  952 NDNIMI-TESGNLFHIDFGHILGNYKsFLGInKERVPFVLTPDFLYVMGTSG 1002
Cdd:cd05171    193 LNNILIdQKTGELVHIDLGIAFEQGK-LLPI-PETVPFRLTRDIVDGMGITG 242
C2_PI3K_class_I_alpha cd08398
C2 domain present in class I alpha phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 353-530 8.61e-12

C2 domain present in class I alpha phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, alpha isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176043  Cd Length: 158  Bit Score: 64.43  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  353 SLWDCNRKFRVKVI-GIDIPVLPRNTelmVFVEANIQHG-QQLLAQRRTTCKPFTEEvLWNTWLDFDIKIKDLPKGALLN 430
Cdd:cd08398      2 SLWKINSNLRIKILcATYVNVNDIDK---IYVRTGIYHGgEPLCDNVNTQRVPCSNP-RWNEWLDYDIYIPDLPRSARLC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  431 LQIYCGKSpsltTKTNVQPHDTLSsdskcknqllyYVNLLLIDHRFLLRQGDYVLHMWKIPgKGEEqgsinaDKL----T 506
Cdd:cd08398     78 LSICSVKG----RKGAKEEHCPLA-----------WGNINLFDYTDTLVSGKMALNLWPVP-HGLE------DLLnpigV 135

                          170       180
                   ....*....|....*....|....
gi 1716990059  507 SATNPDKETSmAISIVLDRYCHPI 530
Cdd:cd08398    136 TGSNPNKDTP-CLELEFDRFSCVV 158
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 805-1002 4.02e-10

Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 62.11  E-value: 4.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  805 KVMASKKKPLWLEFKCADptalsnetiGIIFK-----HgDDLRQDMLILQILR----IMESIWEAEALDLCLLPYGCIST 875
Cdd:cd05169      9 EVITSKQRPRKLTIVGSD---------GKEYKfllkgH-EDLRLDERVMQLFGlvntLLKNDSETSRRNLSIQRYSVIPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  876 GNKIGMIEIVKDATTIAKI---------------QQSTVGNTGAF-------KDEVLNQ--------------WLKEKCP 919
Cdd:cd05169     79 SPNSGLIGWVPGCDTLHSLirdyrekrkiplnieHRLMLQMAPDYdnltliqKVEVFEYalentpgddlrrvlWLKSPSS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  920 veekfCASVER---FVYSCAGYCVATYVLGIGDRHNDNIMI-TESGNLFHIDFGhilgnyKSF-LGINK----ERVPFVL 990
Cdd:cd05169    159 -----EAWLERrtnFTRSLAVMSMVGYILGLGDRHPSNIMLdRLTGKVIHIDFG------DCFeVAMHRekfpEKVPFRL 227

                          250
                   ....*....|..
gi 1716990059  991 TPDFLYVMGTSG 1002
Cdd:cd05169    228 TRMLVNAMEVSG 239
PI3K_C2 pfam00792
Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 ...
 381-488 4.12e-10

Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 domain. Outlier of pfam00168 family.


Pssm-ID: 395640  Cd Length: 136  Bit Score: 58.92  E-value: 4.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  381 VFVEANIQHGQQLLAQR-RTTCKPF-TEEVLWNTWLDFDIKIKDLPKGALLNLQIYCGKSPSLTTKtnvqphdtlssdsk 458
Cdd:pfam00792    5 LYVECQLYHGGKPLCLPvSTRYVPFsNSSIKWNEWITFPIQISDLPRSARLCITIWDVSGPEKSFV-------------- 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 1716990059  459 cknqLLYYVNLLLIDHRFLLRQGDYVLHMW 488
Cdd:pfam00792   71 ----PIGWVNTSLFDKKGILRQGKQKLRLW 96
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 835-1002 1.06e-09

Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical role in the mRNA surveillance mechanism known as non-sense mediated mRNA decay (NMD). NMD protects the cells from the accumulation of aberrant mRNAs with premature termination codons (PTCs) generated by genome mutations and by errors during transcription and splicing. SMG-1 phosphorylates Upf1, another central component of NMD, at the C-terminus upon recognition of PTCs. The phosphorylation/dephosphorylation cycle of Upf1 is essential for promoting NMD. In addition to its catalytic domain, SMG-1 contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. SMG-1 is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The SMG-1 catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270714  Cd Length: 304  Bit Score: 61.12  E-value: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  835 FKHGDDLRQDMLILQILRI----MESIWEAEALDLCLLPYGCISTGNKIGMIEIVKDATTI-----------AKIQQSTV 899
Cdd:cd05170     34 FKGLEDLHLDERIMQFLSIvnamLASDNEHRRRRYRARHYSVTPLGPRSGLIQWVDGATPLfslykrwqqrrAAAQAQKN 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  900 GNTGAFKDEV----------LNQWLKEK----------CPVE--------------------EKFCAS---------VER 930
Cdd:cd05170    114 QDSGSTPPPVprpselfynkLKPALKAAgirkstsrreWPLEvlrqvleelvaetprdllarELWCSSpssaewwrvTQR 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  931 FVYSCAGYCVATYVLGIGDRHNDNIMIT-ESGNLFHIDF------GHILgnyksflginK--ERVPFVLTPDFLYVMGTS 1001
Cdd:cd05170    194 FARSLAVMSMIGYIIGLGDRHLDNILVDlSTGEVVHIDYnvcfekGKRL----------RvpEKVPFRLTQNIEHALGPT 263


                   .
gi 1716990059 1002 G 1002
Cdd:cd05170    264 G 264
C2A_PI3K_class_II cd04012
C2 domain first repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 ...
 382-488 6.89e-09

C2 domain first repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. Class II PIK3s act downstream of receptors for growth factors, integrins, and chemokines. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175979  Cd Length: 171  Bit Score: 56.21  E-value: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  382 FVEANIQHGQQLL-----AQRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALLNLQIYcGKSPSLTTKTNVQPHDTlssd 456
Cdd:cd04012     32 YLSCSLYHGGRLLcspvtTKPVKITKSFFPRVVWDEWIEFPIPVCQLPRESRLVLTLY-GTTSSPDGGSNKQRMGP---- 106

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1716990059  457 skcknQLLYYVNLLLIDHRFLLRQGDYVLHMW 488
Cdd:cd04012    107 -----EELGWVSLPLFDFRGVLRQGSLLLGLW 133
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
 930-1002 5.74e-04

Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs to the the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. It contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain and has a large molecular weight. Unlike most PIKK proteins, however, it contains an inactive PI3K-like pseudokinase domain, which lacks the conserved residues necessary for ATP binding and catalytic activity. TRRAP also contains many motifs that may be critical for protein-protein interactions. TRRAP is a common component of many histone acetyltransferase (HAT) complexes, and is responsible for the recruitment of these complexes to chromatin during transcription, replication, and DNA repair. TRRAP also exists in non-HAT complexes such as the p400 and MRN complexes, which are implicated in ATP-dependent remodeling and DNA repair, respectively. The TRRAP pseudokinase domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270707  Cd Length: 252  Bit Score: 42.89  E-value: 5.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1716990059  930 RFVYSCAGYCVATYVLGIGDRHNDNIMITE-SGNLFHIDFGHILGNYKSFLGINkERVPFVLTPD---FLYVMGTSG 1002
Cdd:cd05163    140 QFTLQLALSSFMTYVLSLGNRTPHRILISRsTGNVFMTDFLPSINSQGPLLDNN-EPVPFRLTPNiqhFIGPIGVEG 215
C2_PI3K_class_III cd08397
C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 375-434 1.05e-03

C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. These are the only domains identified in the class III PI3Ks present in this cd. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176042  Cd Length: 159  Bit Score: 41.08  E-value: 1.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1716990059  375 RNTELmvFVEANIQHGQQLLA-QRRTTCKPFTEEVLWNTWLDFDIKIKDLPKGALLNLQIY 434
Cdd:cd08397     28 PNSDL--FVTCQVFDDGKPLTlPVQTSYKPFKNRRNWNEWLTLPIKYSDLPRNSQLAITIW 86
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 847-979 2.01e-03

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 42.38  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716990059  847 ILQILrIMESIWEAEALDLCLLPYGCIStgnkiGMIEivkdattiaKIQQSTVGNTGAFkdEVLNQWLKEKCPVEEKFCA 926
Cdd:PTZ00303  1073 LLQML-LSSEIGNAEMLDYSVLPLSCDS-----GLIE---------KAEGRELSNLDNM--DIASYVLYRGTRSCINFLA 1135

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1716990059  927 SVERFVyscagycVATYVLGIGDRHNDNIMITESGNLFHIDFGHILGNyKSFL 979
Cdd:PTZ00303  1136 SAKLFL-------LLNYIFSIGDRHKGNVLIGTNGALLHIDFRFIFSE-KTFV 1180
 
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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