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Conserved domains on  [gi|386763732|ref|NP_570014|]
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phosphatidylinositol 4-kinase III alpha, isoform C [Drosophila melanogaster]

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List of domain hits

Name Accession Description Interval E-value
PI4Kc_III_alpha cd05167
Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; The PI4K ...
1808-2133 0e+00

Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; 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. 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.


:

Pssm-ID: 119427 [Multi-domain]  Cd Length: 311  Bit Score: 606.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1808 YLPSNPEAMVLDIDYSSGTPMQSAAKAPYLARFRVYRCGITELEtramevsnnpnsqedaKMTLGVESWQAAIFKVGDDV 1887
Cdd:cd05167     1 YLPSNPDYVIVGIDYKSGTPLQSHAKAPILVTFKVKDRGGDELE----------------EVDDGKVSWQACIFKVGDDC 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1888 RQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQHQYGDESSKEFQAA 1967
Cdd:cd05167    65 RQDMLALQLISLFKNIFQSAGLDLYLFPYRVVATGPGCGVIEVVPNSKSRDQIGRTTDNGLYEYFTSKYGDESSLAFQKA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1968 RANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPGGNIGFE-PDMKLTDEMVMIMGGKMDSPAFK 2046
Cdd:cd05167   145 RENFIRSMAAYSLISYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPGGNLKFEsAPFKLTKEMVQIMGGSMEATPFK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2047 WFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRGQTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQ 2126
Cdd:cd05167   225 WFVELCVRAFLAVRPYMDEIVSLVELMLDSGLPCFRGDTIKNLRQRFAPEKSEREAAEFMLSLIAESYEKFRTKGYDQFQ 304

                  ....*..
gi 386763732 2127 YYQNQIP 2133
Cdd:cd05167   305 YYQNGIP 311
PI4Ka cd00871
Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 ...
1580-1755 1.21e-92

Phosphoinositide 4-kinase(PI4K), 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. PI4K phosphorylates hydroxylgroup at position 4 on the inositol ring of phosphoinositide, the first commited step in the phosphatidylinositol cycle.


:

Pssm-ID: 238443  Cd Length: 175  Bit Score: 300.04  E-value: 1.21e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1580 AWCYNPALAVFLPQRIKNaEIIDEEVSRLVCSDPIAVCHIPEALKYLCTTKNLLQESPDLVYILSWSPVTPIQALAYFSR 1659
Cdd:cd00871     1 AWAISPRLAIHLPSRFPN-SKLKSEVTRLVRKHPLAVVKIPEALPFLVTGKSVDENSPDLKYLLYWAPVSPVQALSLFTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1660 QYPSHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDTMGYVVEFIKNISRRSQIVAHQLIWNMQTNMYMDEDQQHKDP 1739
Cdd:cd00871    80 QYPGHPLVLQYAVRVLESYPVETVFFYIPQIVQALRYDKMGYVEEYILETAKRSQLFAHQIIWNMQTNCYKDEEGKPKDP 159
                         170
                  ....*....|....*.
gi 386763732 1740 NLYEALDQLSQSIIAS 1755
Cdd:cd00871   160 AIKPTLDRVMEKIIDS 175
 
Name Accession Description Interval E-value
PI4Kc_III_alpha cd05167
Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; The PI4K ...
1808-2133 0e+00

Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; 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. 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.


Pssm-ID: 119427 [Multi-domain]  Cd Length: 311  Bit Score: 606.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1808 YLPSNPEAMVLDIDYSSGTPMQSAAKAPYLARFRVYRCGITELEtramevsnnpnsqedaKMTLGVESWQAAIFKVGDDV 1887
Cdd:cd05167     1 YLPSNPDYVIVGIDYKSGTPLQSHAKAPILVTFKVKDRGGDELE----------------EVDDGKVSWQACIFKVGDDC 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1888 RQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQHQYGDESSKEFQAA 1967
Cdd:cd05167    65 RQDMLALQLISLFKNIFQSAGLDLYLFPYRVVATGPGCGVIEVVPNSKSRDQIGRTTDNGLYEYFTSKYGDESSLAFQKA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1968 RANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPGGNIGFE-PDMKLTDEMVMIMGGKMDSPAFK 2046
Cdd:cd05167   145 RENFIRSMAAYSLISYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPGGNLKFEsAPFKLTKEMVQIMGGSMEATPFK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2047 WFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRGQTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQ 2126
Cdd:cd05167   225 WFVELCVRAFLAVRPYMDEIVSLVELMLDSGLPCFRGDTIKNLRQRFAPEKSEREAAEFMLSLIAESYEKFRTKGYDQFQ 304

                  ....*..
gi 386763732 2127 YYQNQIP 2133
Cdd:cd05167   305 YYQNGIP 311
PI4Ka cd00871
Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 ...
1580-1755 1.21e-92

Phosphoinositide 4-kinase(PI4K), 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. PI4K phosphorylates hydroxylgroup at position 4 on the inositol ring of phosphoinositide, the first commited step in the phosphatidylinositol cycle.


Pssm-ID: 238443  Cd Length: 175  Bit Score: 300.04  E-value: 1.21e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1580 AWCYNPALAVFLPQRIKNaEIIDEEVSRLVCSDPIAVCHIPEALKYLCTTKNLLQESPDLVYILSWSPVTPIQALAYFSR 1659
Cdd:cd00871     1 AWAISPRLAIHLPSRFPN-SKLKSEVTRLVRKHPLAVVKIPEALPFLVTGKSVDENSPDLKYLLYWAPVSPVQALSLFTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1660 QYPSHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDTMGYVVEFIKNISRRSQIVAHQLIWNMQTNMYMDEDQQHKDP 1739
Cdd:cd00871    80 QYPGHPLVLQYAVRVLESYPVETVFFYIPQIVQALRYDKMGYVEEYILETAKRSQLFAHQIIWNMQTNCYKDEEGKPKDP 159
                         170
                  ....*....|....*.
gi 386763732 1740 NLYEALDQLSQSIIAS 1755
Cdd:cd00871   160 AIKPTLDRVMEKIIDS 175
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
1880-2084 1.48e-67

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  Cd Length: 240  Bit Score: 230.65  E-value: 1.48e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1880 IFKVGDDVRQDMLALQVITIFKNIFQQ----VGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQL--------------- 1940
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQKdketRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeyrkqkgkvldlr 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1941 -----------------GRQTDSGLSEYFQHQYGDESSKeFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHI 2003
Cdd:smart00146   82 sqtatrlkklelfleatGKFPDPVLYDWFTKKFPDPSED-YFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGHL 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   2004 IHIDFGFMFESSPG-GNIGFEPDMKLTDEMVMIMGgkmDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFR 2082
Cdd:smart00146  161 FHIDFGFILGNGPKlFGFPERVPFRLTPEMVDVMG---DSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237

                    ..
gi 386763732   2083 GQ 2084
Cdd:smart00146  238 SG 239
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
1876-2082 2.46e-60

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


Pssm-ID: 249872  Cd Length: 232  Bit Score: 209.50  E-value: 2.46e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1876 WQAAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGR------------- 1942
Cdd:pfam00454    1 GYPFIFKGGDDLRQDERVLQLIGLMNKLLSGEGADRELAAYLVIPLGPGSGLIEWVPNSTTLAEIPRtymvkkgiplfny 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1943 -------------QTDSGLSEYFQHQYGDESskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDK-DGHIIHIDF 2008
Cdd:pfam00454   81 srkvlvfesrtalFPKVGLLQWFVKHFPDAE--EWGEARKNFVRSCAGMSVLDYILGNGDRHLDNILVDKtTGKLFHIDF 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386763732  2009 GFMFESSPGGNIGFEPDMKLTDEMVMIMGGKmDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFR 2082
Cdd:pfam00454  159 GLCFPKAKRLPKPERVPFRLTRPFVEAMGGD-PSGDEGLFRELCETAYEALRRNLNLLTNLLLLFLEDGLPDWR 231
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
1594-1765 1.06e-21

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: 144268  Cd Length: 185  Bit Score: 95.85  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1594 RIKNAEIIDEEVSRLVCSDPIA----------------VCHIPEAL-KYL-CTTKNLLQES-PDLVYILSWSPVTPIQAL 1654
Cdd:pfam00613    2 DLKPNEKERKQLEAILAYDPLSeltaeekdllwkfrysLMSVPKALtKLLlSVKWSDLDEVaQALSLMLKWAPIDPVDAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1655 AYFSRQYPsHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDT--MGYVVEFIKNISRRSQIVAHQLIWNMQTNMYmde 1732
Cdd:pfam00613   82 ELLDPNFP-DPEVRAYAVKCLESASDDELLFYLLQLVQALKYEPfhDSYLSRFLLQRALKNQRLGHFFFWYLKSEIH--- 157
                          170       180       190
                   ....*....|....*....|....*....|...
gi 386763732  1733 dqqhkDPNLYEALDQLSQSIIASFSGAAKRFYE 1765
Cdd:pfam00613  158 -----DKDVSERFGVLLESYLRSCGTSLKGLNK 185
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
1618-1756 4.28e-21

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: 93.86  E-value: 4.28e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1618 HIPEAL-KYL-CTTKNLLQESPDLVYIL-SWSPVTPIQALAYFSRQYPsHPLTAQYAVKTLSSYPAESVLPYIPQLVQAL 1694
Cdd:smart00145   41 NNPKALpKFLlSVKWSDADEVAQALSLLlSWAPLDPEDALELLDPKFP-DPFVRAYAVKRLESASDEELLLYLLQLVQAL 119
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386763732   1695 RHDT--MGYVVEFIKNISRRSQIVAHQLIWNMQTNMYmDEDQQHKDPNLYEA-LDQLSQSIIASF 1756
Cdd:smart00145  120 KYEPylDSALARFLLERALANQRLGHFFYWYLKSELH-DPHVSIRFGLLLEAyLRGCGTHLKELL 183
TEL1 COG5032
Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction ...
1682-2134 2.51e-57

Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction mechanisms / Cell division and chromosome partitioning / Chromatin structure and dynamics / DNA replication, recombination, and repair / Intracellular trafficking and secretion]


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 219.27  E-value: 2.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1682 SVLPYIPQLVQALRHDTMGYVVEFIKNISRRS--QIV--------------------------AHQLIWNMQTNMYMDED 1733
Cdd:COG5032  1548 SVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHpqALVftlrsaiestalskesvalslenksrTHDPSLVKEALELSDEN 1627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1734 ----QQHKDPNLYEALDQLSQSI-----IASFSGAAKRFYEREFDFF----GKITAVSGEIRSFAKGIERKNACLAALSR 1800
Cdd:COG5032  1628 iriaYPLLHLLFEPILAQLLSRLssennKISVALLIDKPLHEERENFpsglSLSSFQSSFLKELIKKSPRKIRKKFKIDI 1707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1801 IKVQGGC-----YLPSNPEAMVLDIDYSSG----TPMQSAAK------APYLARFRVYRCGITELETRAM-EVSNNPNSq 1864
Cdd:COG5032  1708 SLLNLSRklyisVLRSIRKRLKRLLELRLKkvspKLLLFHAFleiklpGQYLLDKPFVLIERFEPEVSVVkSHLQRPRR- 1786
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1865 EDAKMTLGvESWQAaIFKVGDDVRQDMLALQVITIFKNIFQQVGL----DLFLFPYRVVATAPGCGVIECVPNAKS---- 1936
Cdd:COG5032  1787 LTIRGSDG-KLYSF-IVKGGDDLRQDELALQLIRLMNKILKKDKEtrrrDLWIRPYKVIPLSPGSGIIEWVPNSDTlhsi 1864
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1937 -RDQLGRQ--------------------------------TDSGLSEYFQHQYGDesSKEFQAARANFVKSMAAYSLIGY 1983
Cdd:COG5032  1865 lREYHKRKnisidqekklaarldnlklllkdefftkatlkSPPVLYDWFSESFPN--PEDWLTARTNFARSLAVYSVIGY 1942
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1984 LLQIKDRHNGNIMIDKD-GHIIHIDFGFMFESSPGgniGFEPDM----KLTDEMVMIMGGKMDSPAFKwfcELCVQAFLA 2058
Cdd:COG5032  1943 ILGLGDRHPGNILIDRSsGHVIHIDFGFILFNAPG---RFPFPEkvpfRLTRNIVEAMGVSGVEGSFR---ELCETAFRA 2016
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2059 VRPYQDAIVSLVSLMLD------TGLPCFRG---QTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQYYQ 2129
Cdd:COG5032  2017 LRKNADSLMNVLELFVRdpliewRRLPCFREiqnNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096

                  ....*
gi 386763732 2130 NQIPY 2134
Cdd:COG5032  2097 MYIGW 2101
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
1970-2012 9.40e-06

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 49.70  E-value: 9.40e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386763732 1970 NFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMF 2012
Cdd:PTZ00303 1132 NFLASAKLFLLLNYIFSIGDRHKGNVLIGTNGALLHIDFRFIF 1174
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
1973-2011 3.96e-04

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].


Pssm-ID: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 43.83  E-value: 3.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 386763732  1973 KSMAAYSLIGYLLQI-------KDRHNGNIMIDKDGHIIHIDFGFM 2011
Cdd:TIGR01982  259 KALAENLARSFLNQVlrdgffhADLHPGNIFVLKDGKIIALDFGIV 304
 
Name Accession Description Interval E-value
PI4Kc_III_alpha cd05167
Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; The PI4K ...
1808-2133 0e+00

Phosphoinositide 4-kinase (PI4K), Type III, alpha isoform, catalytic domain; 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. 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.


Pssm-ID: 119427 [Multi-domain]  Cd Length: 311  Bit Score: 606.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1808 YLPSNPEAMVLDIDYSSGTPMQSAAKAPYLARFRVYRCGITELEtramevsnnpnsqedaKMTLGVESWQAAIFKVGDDV 1887
Cdd:cd05167     1 YLPSNPDYVIVGIDYKSGTPLQSHAKAPILVTFKVKDRGGDELE----------------EVDDGKVSWQACIFKVGDDC 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1888 RQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQHQYGDESSKEFQAA 1967
Cdd:cd05167    65 RQDMLALQLISLFKNIFQSAGLDLYLFPYRVVATGPGCGVIEVVPNSKSRDQIGRTTDNGLYEYFTSKYGDESSLAFQKA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1968 RANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPGGNIGFE-PDMKLTDEMVMIMGGKMDSPAFK 2046
Cdd:cd05167   145 RENFIRSMAAYSLISYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPGGNLKFEsAPFKLTKEMVQIMGGSMEATPFK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2047 WFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRGQTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQ 2126
Cdd:cd05167   225 WFVELCVRAFLAVRPYMDEIVSLVELMLDSGLPCFRGDTIKNLRQRFAPEKSEREAAEFMLSLIAESYEKFRTKGYDQFQ 304

                  ....*..
gi 386763732 2127 YYQNQIP 2133
Cdd:cd05167   305 YYQNGIP 311
PI4Ka cd00871
Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 ...
1580-1755 1.21e-92

Phosphoinositide 4-kinase(PI4K), 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. PI4K phosphorylates hydroxylgroup at position 4 on the inositol ring of phosphoinositide, the first commited step in the phosphatidylinositol cycle.


Pssm-ID: 238443  Cd Length: 175  Bit Score: 300.04  E-value: 1.21e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1580 AWCYNPALAVFLPQRIKNaEIIDEEVSRLVCSDPIAVCHIPEALKYLCTTKNLLQESPDLVYILSWSPVTPIQALAYFSR 1659
Cdd:cd00871     1 AWAISPRLAIHLPSRFPN-SKLKSEVTRLVRKHPLAVVKIPEALPFLVTGKSVDENSPDLKYLLYWAPVSPVQALSLFTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1660 QYPSHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDTMGYVVEFIKNISRRSQIVAHQLIWNMQTNMYMDEDQQHKDP 1739
Cdd:cd00871    80 QYPGHPLVLQYAVRVLESYPVETVFFYIPQIVQALRYDKMGYVEEYILETAKRSQLFAHQIIWNMQTNCYKDEEGKPKDP 159
                         170
                  ....*....|....*.
gi 386763732 1740 NLYEALDQLSQSIIAS 1755
Cdd:cd00871   160 AIKPTLDRVMEKIIDS 175
PI4Kc_III cd00893
Phosphoinositide 4-kinase (PI4K), Type III, catalytic domain; The PI4K catalytic domain family ...
1818-2133 3.29e-125

Phosphoinositide 4-kinase (PI4K), Type III, catalytic domain; 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. 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.


Pssm-ID: 119419 [Multi-domain]  Cd Length: 289  Bit Score: 397.19  E-value: 3.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1818 LDIDYSSGTPMQSAAKAPYLARFRVYRCGITeletramevsnnpnsqedakmtlgvesWQAAIFKVGDDVRQDMLALQVI 1897
Cdd:cd00893     1 LSKIYISPKILQSALKIPYLELKKLTDSTLI---------------------------NSEFIVKCGDDLRQDILATQII 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1898 TIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQHQYGDESSKEFQAARANFVKSMAA 1977
Cdd:cd00893    54 TELQKIFELMFLDLWLNPYLVLPVSKTGGIIEFIPNSISIHEIKKQQINSLYDYFLELYGSYTTEAFLQARYNFIESMAG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1978 YSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPGGNIGFEP-DMKLTDEMVMIMGGKMDSPaFKWFCELCVQAF 2056
Cdd:cd00893   134 YSLLCYLLQIKDRHNGNILLDSDGHIIHIDFGFILDSSPGNNLGFEPaAFKFTKEMVDFMGGKKSDD-FKKFRYLCLRGF 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386763732 2057 LAVRPYQDAIVSLVSLMLDTGLPCFRGQTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQYYQNQIP 2133
Cdd:cd00893   213 IAVRKHMDLVISLVYLLIFSGLPCFRGSTIKKLKERLCLNMSEKEAINTVMKKIDSSYNSITTKLYDKVQYYQNGII 289
PI4Kc_III_beta cd05168
Phosphoinositide 4-kinase (PI4K), Type III, beta isoform, catalytic domain; The PI4K catalytic ...
1874-2132 3.98e-98

Phosphoinositide 4-kinase (PI4K), Type III, beta isoform, catalytic domain; 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. 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.


Pssm-ID: 119428 [Multi-domain]  Cd Length: 293  Bit Score: 320.29  E-value: 3.98e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1874 ESWQ--AAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSG---L 1948
Cdd:cd05168    28 KSWDlrSVIVKTGDDLRQELLAMQLIQQFDRIFKEEGLPLWLRPYEILVTSSNSGLIETIPDTVSIDSLKKKLTSKfksL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1949 SEYFQHQYGDESSKeFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPgGNIGFE--PdM 2026
Cdd:cd05168   108 LDFFKKTFGDPSER-FREAQKNFIESLAGYSLICYLLQIKDRHNGNILIDNDGHIIHIDFGFMLSNSP-GNVGFEtaP-F 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2027 KLTDEMVMIMGGkMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLML-DTGLPCFRG--QTINLLKQRFVATKNNKEAA 2103
Cdd:cd05168   185 KLTQEYIEVMGG-VNSDLFNYFKKLFLKGFMALRKHVDRIILLVEIMQsDSKLPCFKAgeFTIQQLRDRFMLNLTEEQLE 263
                         250       260
                  ....*....|....*....|....*....
gi 386763732 2104 AHMLAVIRNSYQNFRTRTYDMIQYYQNQI 2132
Cdd:cd05168   264 VFVDELINQSLDNWRTRLYDKFQYLTNGI 292
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
1880-2084 1.48e-67

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  Cd Length: 240  Bit Score: 230.65  E-value: 1.48e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1880 IFKVGDDVRQDMLALQVITIFKNIFQQ----VGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQL--------------- 1940
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQKdketRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeyrkqkgkvldlr 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1941 -----------------GRQTDSGLSEYFQHQYGDESSKeFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHI 2003
Cdd:smart00146   82 sqtatrlkklelfleatGKFPDPVLYDWFTKKFPDPSED-YFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGHL 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   2004 IHIDFGFMFESSPG-GNIGFEPDMKLTDEMVMIMGgkmDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFR 2082
Cdd:smart00146  161 FHIDFGFILGNGPKlFGFPERVPFRLTPEMVDVMG---DSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237

                    ..
gi 386763732   2083 GQ 2084
Cdd:smart00146  238 SG 239
PI3Kc cd00891
Phosphoinositide 3-kinase (PI3K), catalytic domain; The PI3K catalytic domain family is part ...
1764-2125 6.37e-62

Phosphoinositide 3-kinase (PI3K), catalytic domain; 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. 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.


Pssm-ID: 119417 [Multi-domain]  Cd Length: 352  Bit Score: 218.63  E-value: 6.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1764 YEREFDFFGKITAVSGEIRSFAKGIERKNACLAALSRIKVQ--GGCYLPSNPEAMVLDIDYSSGTPMQSAAKAPYLArfr 1841
Cdd:cd00891     4 LLKQVEVINELKTLAKKVKREKSKSQRKELLREELKKLENNlpQEFTLPLDPRLEIKGLIIEKCKVMDSKKKPLWLV--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1842 vyrcgiteletrameVSNNPNSQEDAKMtlgveswqaaIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVAT 1921
Cdd:cd00891    81 ---------------FKNADPSGEPIKV----------IFKVGDDLRQDMLTLQMIRLMDKIWKKEGLDLRMTPYGCIAT 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1922 APGCGVIECVPNA--------KSRDQLGRQTDSGLSEYFQHQYGDEssKEFQAARANFVKSMAAYSLIGYLLQIKDRHNG 1993
Cdd:cd00891   136 GDGVGMIEVVPNSetiakiqkKAGGVGGAFKDNPLMNWLKKKNKGE--EDYEKAVENFTYSCAGYCVATYVLGIGDRHND 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1994 NIMIDKDGHIIHIDFG-FMfesspgGNI----GFEPD---MKLTDEMVMIMGGKmDSPAFKWFCELCVQAFLAVRPYQDA 2065
Cdd:cd00891   214 NIMLTKTGHLFHIDFGhFL------GNFkkkfGIKRErapFVLTPDMAYVMGGG-DSEKFQRFEDLCCKAYNILRKHGNL 286
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763732 2066 IVSLVSLMLDTGLPCFRG-QTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMI 2125
Cdd:cd00891   287 FINLFSLMLSAGIPELQSiEDIEYLRDALALDKSDEEATEYFRKLIHESLNSKTTKVNNFI 347
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
1876-2082 2.46e-60

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


Pssm-ID: 249872  Cd Length: 232  Bit Score: 209.50  E-value: 2.46e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1876 WQAAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGR------------- 1942
Cdd:pfam00454    1 GYPFIFKGGDDLRQDERVLQLIGLMNKLLSGEGADRELAAYLVIPLGPGSGLIEWVPNSTTLAEIPRtymvkkgiplfny 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1943 -------------QTDSGLSEYFQHQYGDESskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDK-DGHIIHIDF 2008
Cdd:pfam00454   81 srkvlvfesrtalFPKVGLLQWFVKHFPDAE--EWGEARKNFVRSCAGMSVLDYILGNGDRHLDNILVDKtTGKLFHIDF 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386763732  2009 GFMFESSPGGNIGFEPDMKLTDEMVMIMGGKmDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFR 2082
Cdd:pfam00454  159 GLCFPKAKRLPKPERVPFRLTRPFVEAMGGD-PSGDEGLFRELCETAYEALRRNLNLLTNLLLLFLEDGLPDWR 231
PI3Kc_like cd00142
Phosphoinositide 3-kinase (PI3K)-like family, catalytic domain; The PI3K-like catalytic domain ...
1876-2076 1.20e-56

Phosphoinositide 3-kinase (PI3K)-like family, catalytic domain; 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. Members of the family include PI3K, phosphoinositide 4-kinase (PI4K), PI3K-related protein kinases (PIKKs), and TRansformation/tRanscription domain-Associated Protein (TRRAP). 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.


Pssm-ID: 119416  Cd Length: 219  Bit Score: 198.63  E-value: 1.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1876 WQAAIFKVGDDVRQDMLALQVITIFKNIFQQV-GLDLFLFPYRVVATAPGCGVIECVPNAKSrdqlgrqTDSGLSEYFQH 1954
Cdd:cd00142    29 EYRILFKNGDDLRQDERVLQFIRLMNKILKKElGLDLFLTTYSVIPLSPRSGLIEVVPGSVT-------LEDDLSKWLKR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1955 QYGDESskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKD-GHIIHIDFGFMFESSPGGNIGFEPDMKLTDEMV 2033
Cdd:cd00142   102 KSPDED--EWQEARENFISSLAGYSVAGYILGIGDRHPDNIMIDLDtGKLFHIDFGFIFGKRKKFLGRERVPFRLTPDLV 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386763732 2034 MIMGGKMdspAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDT 2076
Cdd:cd00142   180 NALGTGG---VFGPFRSLCVKAMLILRRHAGLLLNLLSLMLRD 219
PI3Kc_III cd00896
Phosphoinositide 3-kinase (PI3K), class III, catalytic domain; The PI3K catalytic domain ...
1765-2127 3.01e-55

Phosphoinositide 3-kinase (PI3K), class III, catalytic domain; 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. 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 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.


Pssm-ID: 119422 [Multi-domain]  Cd Length: 350  Bit Score: 198.99  E-value: 3.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1765 EREFDFFGKITAVSGEIRSF----AKGIERKNACLaalSRIKVQ-----GGCYLPSNPEAMVLDIDYSSGTPMQSAaKAP 1835
Cdd:cd00896     5 SRQIEFVDRLRKLLKELRSSkidrPKKIEKLKQLL---SSIEYEllldfEPIPLPLDPSIEITGIIPEESSVFKSA-LMP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1836 YLARFRVYrcgiteletramevsnNPNSQEDAKMtlgveswqaaIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFP 1915
Cdd:cd00896    81 LKLTFKTE----------------KGNEEGEYPV----------IFKVGDDLRQDQLVIQIISLMDRLLKKENLDLKLTP 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1916 YRVVATAPGCGVIECVPNAKSRDQLgrQTDSGLSEYFQHQYGDESSKEFQAARA--NFVKSMAAYSLIGYLLQIKDRHNG 1993
Cdd:cd00896   135 YKVLATSPTDGLVEFIPSVTLASIL--KKYGGILNYLRKLNPDDGGPLGISPEVmdTFVKSCAGYCVITYILGVGDRHLD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1994 NIMIDKDGHIIHIDFGFMFESSPGgniGFEPDMKLTDEMVMIMGGKmDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLM 2073
Cdd:cd00896   213 NLLLTKDGKLFHIDFGYILGRDPK---PFPPPMKLCKEMVEAMGGA-QSEGYQEFKSYCCEAYNILRKSANLILNLFSLM 288
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386763732 2074 LDTGLPCFRGQ---TINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMI----QY 2127
Cdd:cd00896   289 VDANIPDIALDpdkAILKVQEKFRLDLSDEEAIKHFQNLINDSVNALFPVVVDRLhawaQY 349
PI3Kc_II cd05166
Phosphoinositide 3-kinase (PI3K), class II, catalytic domain; The PI3K catalytic domain family ...
1766-2120 3.50e-44

Phosphoinositide 3-kinase (PI3K), class II, catalytic domain; 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. 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.


Pssm-ID: 119426 [Multi-domain]  Cd Length: 353  Bit Score: 166.85  E-value: 3.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1766 REFDFFGKITAVSGEIRSfAKGIERKNACLAALSRIK---VQGGCYLPSNPEAMVLDIDYSSGTPMQSAAKaPYLARFRv 1842
Cdd:cd05166     6 KQHKLVNKLGSIAEDVKS-ASESARQHVLRTGLGRVDsflLQNKCRLPLNPALDVKGIDVRECSYFNSNAL-PLKISFV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1843 yrcgiteletramevsnNPNSqedakmtLGVESwqAAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATA 1922
Cdd:cd05166    83 -----------------NADP-------MGENI--SVIFKAGDDLRQDMLVLQMINIMDKIWLQEGLDLRMITFRCLSTG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1923 PGCGVIECVPNAKSRDQLGRQ-------TDSGLSEYFQHQYGDESskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNI 1995
Cdd:cd05166   137 YDRGMVELVPDAETLRKIQVEegltgsfKDRPIAKWLMKHNPSEL--EYEKAVENFIYSCAGCCVATYVLGICDRHNDNI 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1996 MIDKDGHIIHIDFG-FMFESSPGGNIGFE-PDMKLTDEMV-MIMGGKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSL 2072
Cdd:cd05166   215 MLTKSGHMFHIDFGkFLGHAQMFGGFKRDrAPFVFTSDMAyVINGGDKPTQRFQDFVDLCCRAYNIIRKHANLLLNLLRM 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386763732 2073 MLDTGLPCFRG-QTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTR 2120
Cdd:cd05166   295 MACSGLPELSKiQDLKYVRDALRPQLTDAEATIQFTKMIQSSLGSAFTK 343
PI3Ka cd00864
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
1580-1730 7.27e-42

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: 153.53  E-value: 7.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1580 AWCYNPALAVFLPQRIKNAEIIDEEVSRLVCSDPIAV-CHIPEALKYLCTtkNLLQESPDLVYILS-WSPVTPIQALAYF 1657
Cdd:cd00864     1 AWERKPLLAILLYPPFSTLTEEEKELLWKFRYYLLNVpKALPKLLKSVNW--NDDEEVSELYQLLKwWAPLSPEDALELL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386763732 1658 SRQYPsHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDT--MGYVVEFIKNISRRSQIVAHQLIWNMQTNMYM 1730
Cdd:cd00864    79 SPKYP-DPVVRQYAVRVLESASDDELLLYLPQLVQALKYEPylDSYLARFLLERALKSQRLGHQLYWNLKSEIHD 152
PI3Kc_IB_gamma cd00894
Phosphoinositide 3-kinase (PI3K), class IB, gamma isoform, catalytic domain; The PI3K ...
1880-2110 3.02e-38

Phosphoinositide 3-kinase (PI3K), class IB, gamma isoform, catalytic domain; 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. 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 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). PI3Kgamma associates with one of two regulatory subunits, p101 and p84. It 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. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility.


Pssm-ID: 119420 [Multi-domain]  Cd Length: 365  Bit Score: 149.26  E-value: 3.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQT--------DSGLSEY 1951
Cdd:cd00894   103 IFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTvgntgafkDEVLSHW 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1952 FQHQYGDEssKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFM---FESSPGGNIGFEPdMKL 2028
Cdd:cd00894   183 LKEKCPIE--EKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHIlgnYKSFLGINKERVP-FVL 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2029 TDEMVMIMG--GKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRG-QTINLLKQRFVATKNNKEAAAH 2105
Cdd:cd00894   260 TPDFLFVMGtsGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSkEDIEYIRDALTVGKSEEDAKKH 339

                  ....*
gi 386763732 2106 MLAVI 2110
Cdd:cd00894   340 FLDQI 344
PI3Kc_I cd05165
Phosphoinositide 3-kinase (PI3K), class I, catalytic domain; The PI3K catalytic domain family ...
1880-2116 3.04e-38

Phosphoinositide 3-kinase (PI3K), class I, catalytic domain; 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. 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. 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).


Pssm-ID: 119425 [Multi-domain]  Cd Length: 366  Bit Score: 149.49  E-value: 3.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQTDSGLSEYFQ----HQ 1955
Cdd:cd05165   102 IFKNGDDLRQDMLTLQILRIMDSIWKEEGLDLRMLPYGCLSTGDKIGLIEVVRDSTTIANIQQETGGNATAAFKkealLH 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1956 YGDESSKE---FQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFM---FESSPGGNIGFEPdMKLT 2029
Cdd:cd05165   182 WLKEKNPTeekLDAAIEEFTLSCAGYCVATFVLGIGDRHNDNIMVKETGQLFHIDFGHIlgnYKSKFGINRERVP-FVLT 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2030 DEMVMIMG---GKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLP---CFrgQTINLLKQRFVATKNNKEAA 2103
Cdd:cd05165   261 PDFVHVIGrgkKDNTSEHFQRFQDLCEKAYLALRRHGNLLIILFSMMLMSGLPeltSK--EDIEYLRDTLALGKSEEEAL 338
                         250
                  ....*....|...
gi 386763732 2104 AHMLAVIRNSYQN 2116
Cdd:cd05165   339 KYFLDKFNEALDG 351
PI3Kc_C2_gamma cd05177
Phosphoinositide 3-kinase (PI3K), class II, gamma isoform, catalytic domain; The PI3K ...
1773-2126 8.76e-35

Phosphoinositide 3-kinase (PI3K), class II, gamma isoform, catalytic domain; 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. 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. The class II gamma isoform, PI3K-C2gamma, is expressed in the liver, breast, and prostate. It's biological function remains unknown.


Pssm-ID: 119436 [Multi-domain]  Cd Length: 354  Bit Score: 138.87  E-value: 8.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1773 KITAVSGEIRSFAKGIERKNACLAALSRIK--VQGG--CYLPSNPEAMVLDIDYSSGTPMQSAAkAPYlarfrvyrcGIT 1848
Cdd:cd05177    12 SILIDAAEKVKTASDTRRKEVLKREASRLEdfFQDVvsCCLPLNPALRVKGIDADACSYFTSNA-APL---------KIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1849 ELETRAMevSNNPNsqedakmtlgveswqaAIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVI 1928
Cdd:cd05177    82 FINANPL--AKNIS----------------IIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGLV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1929 ECVPNAKSRDQLGRQT-------DSGLSEYFQHQYGDESSkeFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDG 2001
Cdd:cd05177   144 QMVPDAVTLAKIHRESgligplkENTIEKWFHMHNKLKED--YDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2002 HIIHIDFG-FMFESSPGGniGFEPDMK---LTDEM--VMIMGGKmdSPA-FKWFCELCVQAFLAVRPYQDAIVSLVSLML 2074
Cdd:cd05177   222 HMFHIDFGkFLGHAQTFG--SIKRDRApfiFTSEMeyFITEGGK--KPQrFQRFVELCCRAYNIVRKHSQLLLNLLEMML 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386763732 2075 DTGLPCFRG-QTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQ 2126
Cdd:cd05177   298 HAGLPELKDiQDLKYVYNNLRPQDTDLEATSYFTKKIKESLECFPVKLNNLIH 350
PI3Kc_C2_alpha cd05176
Phosphoinositide 3-kinase (PI3K), class II, alpha isoform, catalytic domain; The PI3K ...
1880-2120 1.69e-33

Phosphoinositide 3-kinase (PI3K), class II, alpha isoform, catalytic domain; 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. 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. 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.


Pssm-ID: 119435 [Multi-domain]  Cd Length: 353  Bit Score: 134.77  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQL-------GRQTDSGLSEYF 1952
Cdd:cd05176    94 MFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPASETLRKIqveygvtGSFKDKPLAEWL 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1953 QhQYgDESSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFG-FMFESSPGGNigFEPDMK---L 2028
Cdd:cd05176   174 R-KY-NPAEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGkFLGHAQMFGS--FKRDRApfvL 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2029 TDEMV-MIMGGKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRG-QTINLLKQRFVATKNNKEAAAHM 2106
Cdd:cd05176   250 TSDMAyVINGGEKPTIRFQLFVDLCCQAYNLIRKHSNLFLNLLSLMTQSGLPELTGvQDLKYVYDALQPQTTDAEATIFF 329
                         250
                  ....*....|....
gi 386763732 2107 LAVIRNSYQNFRTR 2120
Cdd:cd05176   330 TRLIESSLGSVATK 343
PI3Kc_C2_beta cd00895
Phosphoinositide 3-kinase (PI3K), class II, beta isoform, catalytic domain; The PI3K catalytic ...
1880-2079 2.54e-32

Phosphoinositide 3-kinase (PI3K), class II, beta isoform, catalytic domain; 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. 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. 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.


Pssm-ID: 119421 [Multi-domain]  Cd Length: 354  Bit Score: 131.28  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQL-------GRQTDSGLSEYF 1952
Cdd:cd00895    95 IFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIqvehgvtGSFKDRPLADWL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1953 Q-HQYGDEsskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFG-FMFESSPGGNIGFE--PDMKL 2028
Cdd:cd00895   175 QkHNPTED---EYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGrFLGHAQMFGNIKRDraPFVFT 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386763732 2029 TDEMVMIMGGKMDSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLP 2079
Cdd:cd00895   252 SDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIP 302
PI3Kc_IA_alpha cd05175
Phosphoinositide 3-kinase (PI3K), class IA, alpha isoform, catalytic domain; The PI3K ...
1880-2125 9.54e-32

Phosphoinositide 3-kinase (PI3K), class IA, alpha isoform, catalytic domain; 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. 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 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. 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.


Pssm-ID: 88554 [Multi-domain]  Cd Length: 366  Bit Score: 129.80  E-value: 9.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLgrQTDSGLSEYFQ------ 1953
Cdd:cd05175   102 IFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQI--QCKGGLKGALQfnshtl 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1954 HQYGDESSK--EFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMFESSPgGNIGFE----PDMK 2027
Cdd:cd05175   180 HQWLKDKNKgeMYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKK-KKFGYKrervPFVL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2028 LTDEMVMIMGGKMD---SPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRG-QTINLLKQRFVATKNNKEAA 2103
Cdd:cd05175   259 TQDFLIVISKGAQEctkTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSfDDIAYIRKTLALDKTEQEAL 338
                         250       260
                  ....*....|....*....|..
gi 386763732 2104 AHMLAVIRNSYQNFRTRTYDMI 2125
Cdd:cd05175   339 EYFMKQMNDAHHGGWTTKMDWI 360
PI3Kc_IA_beta cd05173
Phosphoinositide 3-kinase (PI3K), class IA, beta isoform, catalytic domain; The PI3K catalytic ...
1880-2102 2.43e-28

Phosphoinositide 3-kinase (PI3K), class IA, beta isoform, catalytic domain; 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. 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 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. In addition, PI3Kbeta can also 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.


Pssm-ID: 119433  Cd Length: 362  Bit Score: 119.30  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKS--RDQLGRQT---------DSGL 1948
Cdd:cd05173    98 IFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAETiaDIQLNSSNvaaaaafnkDALL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1949 SEYFQHQYGDesskEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFM---FESSPGGNIGFEPD 2025
Cdd:cd05173   178 NWLKEYNSGD----DLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHIlgnFKSKFGIKRERVPF 253
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386763732 2026 MKLTDEMVMIMGGKM-DSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFRG-QTINLLKQRFVATKNNKEA 2102
Cdd:cd05173   254 ILTYDFIHVIQQGKTgNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAGLPELTSvKDIQYLKDSLALGKSEEEA 332
PI3Kc_IA_delta cd05174
Phosphoinositide 3-kinase (PI3K), class IA, delta isoform, catalytic domain; The PI3K ...
1862-2105 3.27e-26

Phosphoinositide 3-kinase (PI3K), class IA, delta isoform, catalytic domain; 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. 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 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. 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.


Pssm-ID: 119434 [Multi-domain]  Cd Length: 361  Bit Score: 112.84  E-value: 3.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1862 NSQEDAKMTLGVeswqaaIFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLG 1941
Cdd:cd05174    86 KNEEAGGGSVGI------IFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLSTGDKTGLIEVVKNSDTIANIQ 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1942 R-QTDSGLSEYFQHQY------GDESSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFG-FM-- 2011
Cdd:cd05174   160 LnKSNMAATAAFNKDAllnwlkSKNPGDALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGhFLgn 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2012 FESSPGGNIGFEPDMKLTDEMVMIMGGKM-DSPAFKWFCELCVQAFLAVRPYQDAIVSLVSLMLDTGLPCFR-GQTINLL 2089
Cdd:cd05174   240 FKTKFGINRERVPFILTYDFVHVIQQGKTnNSEKFERFRGYCEQAYKILRRHGTLFLHLFALMKAAGLPELNcSKDIQYL 319
                         250
                  ....*....|....*.
gi 386763732 2090 KQRFVATKNNKEAAAH 2105
Cdd:cd05174   320 KDSLALGKTEEEALKH 335
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
1594-1765 1.06e-21

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: 144268  Cd Length: 185  Bit Score: 95.85  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1594 RIKNAEIIDEEVSRLVCSDPIA----------------VCHIPEAL-KYL-CTTKNLLQES-PDLVYILSWSPVTPIQAL 1654
Cdd:pfam00613    2 DLKPNEKERKQLEAILAYDPLSeltaeekdllwkfrysLMSVPKALtKLLlSVKWSDLDEVaQALSLMLKWAPIDPVDAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732  1655 AYFSRQYPsHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRHDT--MGYVVEFIKNISRRSQIVAHQLIWNMQTNMYmde 1732
Cdd:pfam00613   82 ELLDPNFP-DPEVRAYAVKCLESASDDELLFYLLQLVQALKYEPfhDSYLSRFLLQRALKNQRLGHFFFWYLKSEIH--- 157
                          170       180       190
                   ....*....|....*....|....*....|...
gi 386763732  1733 dqqhkDPNLYEALDQLSQSIIASFSGAAKRFYE 1765
Cdd:pfam00613  158 -----DKDVSERFGVLLESYLRSCGTSLKGLNK 185
PIKKc cd05164
Phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily, catalytic domain; The PIKK ...
1880-2070 2.68e-21

Phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily, catalytic domain; 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. 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.


Pssm-ID: 119424  Cd Length: 222  Bit Score: 95.46  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQVGLDLFLF----PYRVVATAPGCGVIECVPNAKS-RDQLGrqtdsglsEYFQH 1954
Cdd:cd05164    33 LVKGGEDLRQDQRIMQLFQFCNTLLAKDAECRRRKltirTYAVIPLNSRSGLIEWVEGTTTlKPVLK--------KWFWL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1955 QYGDesSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKD-GHIIHIDFGFMFESSPGGNIGFEPDMKLTDEMV 2033
Cdd:cd05164   105 QFPD--PEQWFAARKNYTRSTAVMSIVGYILGLGDRHLDNILIDREtGEVVHIDFGCIFEKGKTLPVPELVPFRLTRNII 182
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 386763732 2034 MIMGGKMDSPAFKwfcELCVQAFLAVRPYQDAIVSLV 2070
Cdd:cd05164   183 NGMGITGVEGLFR---KICEQTLEVFRKHRDTLIAFL 216
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
1618-1756 4.28e-21

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: 93.86  E-value: 4.28e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732   1618 HIPEAL-KYL-CTTKNLLQESPDLVYIL-SWSPVTPIQALAYFSRQYPsHPLTAQYAVKTLSSYPAESVLPYIPQLVQAL 1694
Cdd:smart00145   41 NNPKALpKFLlSVKWSDADEVAQALSLLlSWAPLDPEDALELLDPKFP-DPFVRAYAVKRLESASDEELLLYLLQLVQAL 119
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386763732   1695 RHDT--MGYVVEFIKNISRRSQIVAHQLIWNMQTNMYmDEDQQHKDPNLYEA-LDQLSQSIIASF 1756
Cdd:smart00145  120 KYEPylDSALARFLLERALANQRLGHFFYWYLKSELH-DPHVSIRFGLLLEAyLRGCGTHLKELL 183
PIKKc_ATM cd05171
Ataxia telangiectasia mutated (ATM), catalytic domain; The ATM catalytic domain subfamily is ...
1875-2074 1.03e-17

Ataxia telangiectasia mutated (ATM), catalytic domain; 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. ATM 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). ATM contains a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. 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.


Pssm-ID: 119431  Cd Length: 279  Bit Score: 85.36  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1875 SWQAAIFKVGDDVRQDMLALQVITIFKNIFQQ----VGLDLFLFPYRVVATAPGCGVIECVPNAKS-------------- 1936
Cdd:cd05171    28 KKYKQLLKGGDDDRQDAVMEQVFQLVNTLLERnketRKRKLRIRTYKVVPLSPRAGILEWVDGTIPlgeylvgatgaher 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1937 ------------RDQLGRQTDSgLSEYFQ-------------HQYGDE---SSKEFQAARANFVKSMAAYSLIGYLLQIK 1988
Cdd:cd05171   108 yrpgdwtarkcrKAMAEVQKES-NEERLKvflkicknfrpvfRYFFLEkflDPQDWFERRLAYTRSVATSSIVGYILGLG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1989 DRHNGNIMIDKD-GHIIHIDFGFMFESspgGNIGFEPDM---KLTDEMVMIMGGKMDSPAFKWFCELCVQAFlavRPYQD 2064
Cdd:cd05171   187 DRHANNILIDEKtAEVVHIDLGIAFEQ---GKILPVPETvpfRLTRDIVDGMGITGVEGVFRRCCEKTLEVL---RDNKD 260
                         250
                  ....*....|
gi 386763732 2065 AIVSLVSLML 2074
Cdd:cd05171   261 AILTILEVLL 270
PIKKc_DNA-PK cd05172
DNA-dependent protein kinase (DNA-PK), catalytic domain; The DNA-PK catalytic domain subfamily ...
1880-2012 9.48e-16

DNA-dependent protein kinase (DNA-PK), catalytic domain; 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. 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). 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.


Pssm-ID: 119432  Cd Length: 235  Bit Score: 78.52  E-value: 9.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1880 IFKVGDDVRQDMLALQVITIFKNIFQQ----VGLDLFLFPYRVVATAPGCGVIECVPNAKSRDQLGRQT--DSGLSEYfq 1953
Cdd:cd05172    33 LVKGGEDLRQDQRIQQLFGVMNNILAQdtacRQRALQLRTYQVIPMTPRFGLIEWLENTTPLKEILKNDllRRALVEM-- 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1954 hqygDESSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMIDK-DGHIIHIDFGFMF 2012
Cdd:cd05172   111 ----SASPEAFLSLRDHFAKSLAAMCVSHWILGIGDRHLSNFLVDLeTGGLVGIDFGHAF 166
PIKKc_ATR cd00892
ATR (Ataxia telangiectasia and Rad3-related), catalytic domain; The ATR catalytic domain ...
1885-2037 3.81e-15

ATR (Ataxia telangiectasia and Rad3-related), catalytic domain; 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. ATR is also referred to as Mei-41 (Drosophila), Esr1/Mec1p (Saccharomyces cerevisiae), Rad3 (Schizosaccharomyces pombe), and FRAP-related protein (human). 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). 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 plays a role in normal cell growth and in response to DNA damage.


Pssm-ID: 119418  Cd Length: 237  Bit Score: 76.90  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1885 DDVRQDMLALQVITIFKNIFQQVGL----DLFLFPYRVVATAPGCGVIECVPNAKS-RDQLGRQTDSGLSEYFQHQYGDE 1959
Cdd:cd00892    38 DDLRKDARLMEFNTLINRLLSKDPEsrrrRLYIRTYAVIPLNEECGIIEWVPNTATlRSILLEIYPPVFHEWFLENFPDP 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1960 SSkeFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMID-KDGHIIHIDFGFMFESspgGNIGFEPDM---KLTDEMVMI 2035
Cdd:cd00892   118 SA--WLKARNAYTRSTAVMSMVGYILGLGDRHGENILFDsNTGDVVHVDFNCLFDK---GETLEVPERvpfRLTQNMVDA 192

                  ..
gi 386763732 2036 MG 2037
Cdd:cd00892   193 MG 194
PIKKc_TOR cd05169
TOR (Target of rapamycin), catalytic domain; The TOR catalytic domain subfamily is part of a ...
1886-2013 3.68e-12

TOR (Target of rapamycin), catalytic domain; 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. 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). 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.


Pssm-ID: 119429  Cd Length: 280  Bit Score: 67.94  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1886 DVRQDMLALQ----VITIFKNIFQQVGLDLFLFPYRVVATAPGCGVIECVPNA-----------KSR--------DQLGR 1942
Cdd:cd05169    39 DLRLDERVMQlfglINTLLKNDSETSKRNLSIQTYSVIPLSPNVGLIGWVPGCdtlhslireyrKKRniplnlehRLMEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1943 QTDSG------LSEYFQHQYGDESSKE--------FQAA--------RANFVKSMAAYSLIGYLLQIKDRHNGNIMIDKD 2000
Cdd:cd05169   119 KSAPDydnltlIQKLEVFEYALNNTPGddlrkilwLKSPsseawlerRTNFTRSLAVMSMVGYILGLGDRHPSNIMIDRL 198
                         170
                  ....*....|....
gi 386763732 2001 -GHIIHIDFGFMFE 2013
Cdd:cd05169   199 tGKVIHIDFGDCFE 212
PIKKc_SMG1 cd05170
Suppressor of morphogenetic effect on genitalia-1 (SMG-1), catalytic domain; The SMG-1 ...
1959-2013 1.19e-08

Suppressor of morphogenetic effect on genitalia-1 (SMG-1), catalytic domain; 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. 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). In addition to its catalytic domain, SMG-1 contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. 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.


Pssm-ID: 119430  Cd Length: 307  Bit Score: 57.45  E-value: 1.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386763732 1959 ESSKEFQAARANFVKSMAAYSLIGYLLQIKDRHNGNIMID-KDGHIIHIDFGFMFE 2013
Cdd:cd05170   185 TTSSEWWSVTQRYARSTAVMSMIGYVIGLGDRHLDNVLIDlKTGEVVHIDYNVCFE 240
PI3Ka_II cd00869
Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is ...
1637-1725 1.73e-07

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: 52.07  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1637 PDLVYIL-SWSPVTPIQALAYFSRQYPSHPLTAQyAVKTLSSYPAESVLPYIPQLVQALRHDTM--GYVVEFIKNISRRS 1713
Cdd:cd00869    57 MDVYQLLhQWAPLRPLIALELLLPKFPDQEVRAH-AVQWLARLSNDELLDYLPQLVQALKFELYlkSALVRFLLSRSLVS 135
                          90
                  ....*....|..
gi 386763732 1714 QIVAHQLIWNMQ 1725
Cdd:cd00869   136 LRFAHELYWLLK 147
PI3Ka_I cd00872
Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all ...
1617-1735 1.25e-04

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: 43.46  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1617 CH-IPEAL-KYLCTTK-NLLQESPDLVYILS-WSPVTPIQALAYFSRQYPShPLTAQYAVKTLSSYPAESVLPYIPQLVQ 1692
Cdd:cd00872    34 CRkKPQALpKLLLSVKwNKRDDVAQMYQLLKrWPKLKPEQALELLDCNFPD-EHVREFAVRCLEKLSDDELLQYLLQLVQ 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386763732 1693 ALRHDTM--GYVVEFIKNISRRSQIVAHQLIWNMQTNMYMDEDQQ 1735
Cdd:cd00872   113 VLKYEPYhdSDLVRFLLKRALRNQRIGHFFFWHLRSEMHNPSVSQ 157
PI3Ka_III cd00870
Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is ...
1620-1697 1.08e-03

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: 40.78  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1620 PEAL-KYL-CTTKNLLQESPDLVYIL-SWSPVTPIQALAYFSRQYpSHPLTAQYAVKTLSSYPAESVLPYIPQLVQALRH 1696
Cdd:cd00870    45 KKALtKFLkSVNWSDEQEVKQALELMpKWAKIDIEDALELLSPYF-TNPVVRKYAVSRLKLASDEELLLYLLQLVQALKY 123

                  .
gi 386763732 1697 D 1697
Cdd:cd00870   124 E 124
TEL1 COG5032
Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction ...
1682-2134 2.51e-57

Phosphatidylinositol kinase and protein kinases of the PI-3 kinase family [Signal transduction mechanisms / Cell division and chromosome partitioning / Chromatin structure and dynamics / DNA replication, recombination, and repair / Intracellular trafficking and secretion]


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 219.27  E-value: 2.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1682 SVLPYIPQLVQALRHDTMGYVVEFIKNISRRS--QIV--------------------------AHQLIWNMQTNMYMDED 1733
Cdd:COG5032  1548 SVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHpqALVftlrsaiestalskesvalslenksrTHDPSLVKEALELSDEN 1627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1734 ----QQHKDPNLYEALDQLSQSI-----IASFSGAAKRFYEREFDFF----GKITAVSGEIRSFAKGIERKNACLAALSR 1800
Cdd:COG5032  1628 iriaYPLLHLLFEPILAQLLSRLssennKISVALLIDKPLHEERENFpsglSLSSFQSSFLKELIKKSPRKIRKKFKIDI 1707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1801 IKVQGGC-----YLPSNPEAMVLDIDYSSG----TPMQSAAK------APYLARFRVYRCGITELETRAM-EVSNNPNSq 1864
Cdd:COG5032  1708 SLLNLSRklyisVLRSIRKRLKRLLELRLKkvspKLLLFHAFleiklpGQYLLDKPFVLIERFEPEVSVVkSHLQRPRR- 1786
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1865 EDAKMTLGvESWQAaIFKVGDDVRQDMLALQVITIFKNIFQQVGL----DLFLFPYRVVATAPGCGVIECVPNAKS---- 1936
Cdd:COG5032  1787 LTIRGSDG-KLYSF-IVKGGDDLRQDELALQLIRLMNKILKKDKEtrrrDLWIRPYKVIPLSPGSGIIEWVPNSDTlhsi 1864
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1937 -RDQLGRQ--------------------------------TDSGLSEYFQHQYGDesSKEFQAARANFVKSMAAYSLIGY 1983
Cdd:COG5032  1865 lREYHKRKnisidqekklaarldnlklllkdefftkatlkSPPVLYDWFSESFPN--PEDWLTARTNFARSLAVYSVIGY 1942
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 1984 LLQIKDRHNGNIMIDKD-GHIIHIDFGFMFESSPGgniGFEPDM----KLTDEMVMIMGGKMDSPAFKwfcELCVQAFLA 2058
Cdd:COG5032  1943 ILGLGDRHPGNILIDRSsGHVIHIDFGFILFNAPG---RFPFPEkvpfRLTRNIVEAMGVSGVEGSFR---ELCETAFRA 2016
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763732 2059 VRPYQDAIVSLVSLMLD------TGLPCFRG---QTINLLKQRFVATKNNKEAAAHMLAVIRNSYQNFRTRTYDMIQYYQ 2129
Cdd:COG5032  2017 LRKNADSLMNVLELFVRdpliewRRLPCFREiqnNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096

                  ....*
gi 386763732 2130 NQIPY 2134
Cdd:COG5032  2097 MYIGW 2101
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
1970-2012 9.40e-06

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 49.70  E-value: 9.40e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386763732 1970 NFVKSMAAYSLIGYLLQIKDRHNGNIMIDKDGHIIHIDFGFMF 2012
Cdd:PTZ00303 1132 NFLASAKLFLLLNYIFSIGDRHKGNVLIGTNGALLHIDFRFIF 1174
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
1973-2011 3.96e-04

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].


Pssm-ID: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 43.83  E-value: 3.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 386763732  1973 KSMAAYSLIGYLLQI-------KDRHNGNIMIDKDGHIIHIDFGFM 2011
Cdd:TIGR01982  259 KALAENLARSFLNQVlrdgffhADLHPGNIFVLKDGKIIALDFGIV 304
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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