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Conserved domains on  [gi|398365009|ref|NP_009694|]
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protein kinase MEC1 [Saccharomyces cerevisiae S288C]

Protein Classification

phosphatidylinositol kinase family protein( domain architecture ID 11472127)

phosphatidylinositol kinase family protein such as the serine/threonine-protein kinase tor2, which is an essential phosphatidylinositol kinase homolog required for G1 progression

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
194-2368 0e+00

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


:

Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1385.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  194 TFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQLKyISLVVDYVCNRTISTALDAPALVCCeqLKF 273
Cdd:COG5032     1 DRLAQIIYALPSLLKDCFTEILLRKSDVRSSLFDLLHVSFLDYKEKDER-LSNVNDLVRNSTQSLLNTISNLIKI--VKF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  274 VLTTMHHFLDNKYGLLdNDPTMAKgILRLYSLCISNDFSKCFVDhfpidqwadfsQSEHFPFTQLTNKALSiVYFDLKRR 353
Cdd:COG5032    78 VLPLKSFFLSPIFAKL-RALPMTK-ILCISADTYCLSLSIKALA-----------DDESLTTILKTIRELL-SKFLLRLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  354 SLPVEALKYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQLSPGFFQRAGNDFK 433
Cdd:COG5032   144 LLFLFIGLLAQKFSEAQSKLFFKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNISDGNYFKVEIGRKL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  434 LILNEASVSIQTCFKTNNITR-LTSWTVILGRLACLESEKFSGTLPNSTKDMDNWYVCH-LCDIEKTGN-----PFVRIN 506
Cdd:COG5032   224 LDHLNALGQILDCQKIAKITKsFRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHfETDLFKTFLvtscfLFFVDE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  507 PNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLLSgILFSLHRIFSHF--QPPKLTDGNGQIN-KSFKLVQKCFMNSNRY 583
Cdd:COG5032   304 ICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRIS-ALSSLLVIFDYHlaLPDAVRLLFGESNdKVFLISELALDSTGRL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  584 LRLLSTRIIP-LFNISDSHNSEDEHTATLIKFLQSQKLpvvKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDySLR 662
Cdd:COG5032   383 LRVLPARVLPsLFEFLLSLLTVLKISGLILEFEISAQL---LCNLIRSSNQLLTSLISPYFLFILPKCIDSSNSEI-SYR 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  663 IMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTILDIFQRYIIPYAIIQYKSDVLS 742
Cdd:COG5032   459 VENLGELKDILGLDRITDYQALSLRLIIVSIQLRSFVFKREAINQIFKQLASIVIKPFLDYPKRLDLPIKIVTVVYVALL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  743 EIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHGLfsldiLETLFLNRAPTFDKGYITAYLPdykTLAEITKLYKN 822
Cdd:COG5032   539 RRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-----QLLAVYGFIRSIDDLYFTVSDP---TLIEILKLPVL 610
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  823 SVTKDAsDSENANMILCSLRFLITNFEKDKrHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTYYE 902
Cdd:COG5032   611 SIVHSA-IIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNFLELIVIAFFPLIRSEIIGIVLISSLFS 688
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  903 KLrvINGISFLIIyapkkSIISALAQIsiclqTGLGLKEVRYEAFRCWHLLVRHLNDEELSTVIDSLIafiLQKWSEFNG 982
Cdd:COG5032   689 KT--WILLKLLLI-----AFISKLISA-----LQGELKMLAPTLFTLFLVLVERYLDVEYSSVSFKLL---LVILVYFGG 753
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  983 KLRNIVYSILDtlikeksdLILKLKPYTTLalvGKPELGILARDGQFARMVNKIRSTTDLIPIFANNLKSSnKYVINQNL 1062
Cdd:COG5032   754 NLESLVLLILD--------LIVMLVEYTEL---GLQESIFIERLSQFFKFKNLSENASRLLPPLMDNLSKS-HELRCVSE 821
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1063 DDIEVYLRRKQTERSIDFTPkkvgqtsDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVT-KHEFKRTTYSEN 1141
Cdd:COG5032   822 DDVSALLIQLLTDRVICFIP-------VINSSLGDSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTdLREFFQTVKSKA 894
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1142 EVYDLNDSVQTIKFLIWVINDILVPAFWQSENpsKQLFVALVIQE---SLKYCGLSSESWDMNHKELY-PNEAKLWEKF- 1216
Cdd:COG5032   895 EVLSMLPFVQSILFEAWNRVDFLLKDFWQEEL--DNLLVALLKELpfmALRDCSILSDLYFMLGRELWnSVSFECWLELm 972
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1217 NSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKRFTLDLLKTGTtENHPLHVFSSLIREDDGSLSNFLlP 1296
Cdd:COG5032   973 NSYKRLLIKSLKSKLHLPTIPILILQMLLDSKNLTEFTEHQLKNLPLPSLSIGF-YESLCSFLAKLLHDEELYFFPLL-F 1050
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1297 YISLDIIIKAEKGTPYADILNGIIIEFDSIFTCNLEGMnnlQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFII 1376
Cdd:COG5032  1051 VSSLETLLSVNYHINQLDLRPNILKHFGSFVRFQLKPH---LVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDAL 1127
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1377 KDTKTTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQITYEEIGDIDSLDGVLR 1456
Cdd:COG5032  1128 GKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPFSLQYLYWHINDIDCADKLQS 1207
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1457 TFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRMLKSMYDHQ--LYSQIISNSSFHSSDGKISLSPDVKEW 1534
Cdd:COG5032  1208 VLAELSLVTGISELLLEESWRRALFSNIKDSLESELEEIIDGMYKSNEDFGalMLLSLSAELWDKILEGRSSCSKSIKLS 1287
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1535 YSIGLEAANLEGNVQTLKNWVEQIESLRNIDDREVLLQYNIAKALIAIS-NEDPLRTQKYI---HNSFRLIGTNFITSSK 1610
Cdd:COG5032  1288 LNIWLDLSIVVSPKDEPELFIKFVELCEASSIRSKLLEKNIQELLEKLEeIKSPLGTLRDRlppPWALLDLKRLLATWRQ 1367
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1611 ETTLLKKQNLLMKLHSLYDL--SFLSSAKDKFEYKSNTTILDYRMERIGADFVP-NHYILSMRKSFDQLKMNEQADADLG 1687
Cdd:COG5032  1368 NAFLRINPELLPLLSSLLNLqsSSLSKQLVSRGSSESAISINSFASVARKHFLPdNQLKKIYQLSNILISEAFLLLRYLL 1447
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1688 KTFFTLAQLARNNARLD-IASESLMHCLERRLPQaelefaeilwkQGENDRALKIVQEIHEKYQENSSVNARDRAAVLLK 1766
Cdd:COG5032  1448 LCRLGRRELKAGLNVWNlTNLELFSDIQESEFFE-----------WGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKK 1516
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1767 FTEWLDLSNNSASEQIIKQYQDIFQIDSKWDK--PYYSIGLYYSRLLERKKAEGYITN-GRFEYRAISYFLLAFEKNTAK 1843
Cdd:COG5032  1517 LNLFELLGSLLSAKDAAGSYYKNFHIFDLEISviPFIPQLLSSLSLLDLNSAQSLLSKiGKEHPQALVFTLRSAIESTAL 1596
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1844 VRENLPkvitfwLDIAAASISEAPGNRKEMLSKATEDICShvEEALQHcptYIWYFVLTQLLSRLLHSHQSsaqiimhIL 1923
Cdd:COG5032  1597 SKESVA------LSLENKSRTHDPSLVKEALELSDENIRI--AYPLLH---LLFEPILAQLLSRLSSENNK-------IS 1658
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1924 LSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLtkaLTRVCLQDVKSITSRSGKSLEKD 2003
Cdd:COG5032  1659 VALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISLLNL---SRKLYISVLRSIRKRLKRLLELR 1735
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2004 FKFdmnVAPSAMVVPvrKNLDIISPLESNSMrgyqpfRPVVSIIRFGSSYKVFSS-LKKPKQLNIIGSDGNIYGIMCK-K 2081
Cdd:COG5032  1736 LKK---VSPKLLLFH--AFLEIKLPGQYLLD------KPFVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKgG 1804
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2082 EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKS-LHD 2160
Cdd:COG5032  1805 DDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKkLAA 1884
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2161 RWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVL 2240
Cdd:COG5032  1885 RLDNLKLLLKDEFFTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVI 1964
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2241 HVDF-DCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD------RNMD 2313
Cdd:COG5032  1965 HIDFgFILFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDpliewrRLPC 2044
                        2170      2180      2190      2200      2210      2220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365009 2314 HS------IQKALKVLRNKIRGIDPQDGLVLSVAGQTETLIQEATSEDNLSKMYIGWLPFW 2368
Cdd:COG5032  2045 FReiqnneIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
 
Name Accession Description Interval E-value
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
194-2368 0e+00

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1385.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  194 TFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQLKyISLVVDYVCNRTISTALDAPALVCCeqLKF 273
Cdd:COG5032     1 DRLAQIIYALPSLLKDCFTEILLRKSDVRSSLFDLLHVSFLDYKEKDER-LSNVNDLVRNSTQSLLNTISNLIKI--VKF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  274 VLTTMHHFLDNKYGLLdNDPTMAKgILRLYSLCISNDFSKCFVDhfpidqwadfsQSEHFPFTQLTNKALSiVYFDLKRR 353
Cdd:COG5032    78 VLPLKSFFLSPIFAKL-RALPMTK-ILCISADTYCLSLSIKALA-----------DDESLTTILKTIRELL-SKFLLRLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  354 SLPVEALKYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQLSPGFFQRAGNDFK 433
Cdd:COG5032   144 LLFLFIGLLAQKFSEAQSKLFFKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNISDGNYFKVEIGRKL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  434 LILNEASVSIQTCFKTNNITR-LTSWTVILGRLACLESEKFSGTLPNSTKDMDNWYVCH-LCDIEKTGN-----PFVRIN 506
Cdd:COG5032   224 LDHLNALGQILDCQKIAKITKsFRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHfETDLFKTFLvtscfLFFVDE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  507 PNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLLSgILFSLHRIFSHF--QPPKLTDGNGQIN-KSFKLVQKCFMNSNRY 583
Cdd:COG5032   304 ICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRIS-ALSSLLVIFDYHlaLPDAVRLLFGESNdKVFLISELALDSTGRL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  584 LRLLSTRIIP-LFNISDSHNSEDEHTATLIKFLQSQKLpvvKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDySLR 662
Cdd:COG5032   383 LRVLPARVLPsLFEFLLSLLTVLKISGLILEFEISAQL---LCNLIRSSNQLLTSLISPYFLFILPKCIDSSNSEI-SYR 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  663 IMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTILDIFQRYIIPYAIIQYKSDVLS 742
Cdd:COG5032   459 VENLGELKDILGLDRITDYQALSLRLIIVSIQLRSFVFKREAINQIFKQLASIVIKPFLDYPKRLDLPIKIVTVVYVALL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  743 EIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHGLfsldiLETLFLNRAPTFDKGYITAYLPdykTLAEITKLYKN 822
Cdd:COG5032   539 RRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-----QLLAVYGFIRSIDDLYFTVSDP---TLIEILKLPVL 610
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  823 SVTKDAsDSENANMILCSLRFLITNFEKDKrHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTYYE 902
Cdd:COG5032   611 SIVHSA-IIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNFLELIVIAFFPLIRSEIIGIVLISSLFS 688
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  903 KLrvINGISFLIIyapkkSIISALAQIsiclqTGLGLKEVRYEAFRCWHLLVRHLNDEELSTVIDSLIafiLQKWSEFNG 982
Cdd:COG5032   689 KT--WILLKLLLI-----AFISKLISA-----LQGELKMLAPTLFTLFLVLVERYLDVEYSSVSFKLL---LVILVYFGG 753
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  983 KLRNIVYSILDtlikeksdLILKLKPYTTLalvGKPELGILARDGQFARMVNKIRSTTDLIPIFANNLKSSnKYVINQNL 1062
Cdd:COG5032   754 NLESLVLLILD--------LIVMLVEYTEL---GLQESIFIERLSQFFKFKNLSENASRLLPPLMDNLSKS-HELRCVSE 821
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1063 DDIEVYLRRKQTERSIDFTPkkvgqtsDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVT-KHEFKRTTYSEN 1141
Cdd:COG5032   822 DDVSALLIQLLTDRVICFIP-------VINSSLGDSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTdLREFFQTVKSKA 894
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1142 EVYDLNDSVQTIKFLIWVINDILVPAFWQSENpsKQLFVALVIQE---SLKYCGLSSESWDMNHKELY-PNEAKLWEKF- 1216
Cdd:COG5032   895 EVLSMLPFVQSILFEAWNRVDFLLKDFWQEEL--DNLLVALLKELpfmALRDCSILSDLYFMLGRELWnSVSFECWLELm 972
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1217 NSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKRFTLDLLKTGTtENHPLHVFSSLIREDDGSLSNFLlP 1296
Cdd:COG5032   973 NSYKRLLIKSLKSKLHLPTIPILILQMLLDSKNLTEFTEHQLKNLPLPSLSIGF-YESLCSFLAKLLHDEELYFFPLL-F 1050
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1297 YISLDIIIKAEKGTPYADILNGIIIEFDSIFTCNLEGMnnlQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFII 1376
Cdd:COG5032  1051 VSSLETLLSVNYHINQLDLRPNILKHFGSFVRFQLKPH---LVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDAL 1127
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1377 KDTKTTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQITYEEIGDIDSLDGVLR 1456
Cdd:COG5032  1128 GKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPFSLQYLYWHINDIDCADKLQS 1207
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1457 TFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRMLKSMYDHQ--LYSQIISNSSFHSSDGKISLSPDVKEW 1534
Cdd:COG5032  1208 VLAELSLVTGISELLLEESWRRALFSNIKDSLESELEEIIDGMYKSNEDFGalMLLSLSAELWDKILEGRSSCSKSIKLS 1287
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1535 YSIGLEAANLEGNVQTLKNWVEQIESLRNIDDREVLLQYNIAKALIAIS-NEDPLRTQKYI---HNSFRLIGTNFITSSK 1610
Cdd:COG5032  1288 LNIWLDLSIVVSPKDEPELFIKFVELCEASSIRSKLLEKNIQELLEKLEeIKSPLGTLRDRlppPWALLDLKRLLATWRQ 1367
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1611 ETTLLKKQNLLMKLHSLYDL--SFLSSAKDKFEYKSNTTILDYRMERIGADFVP-NHYILSMRKSFDQLKMNEQADADLG 1687
Cdd:COG5032  1368 NAFLRINPELLPLLSSLLNLqsSSLSKQLVSRGSSESAISINSFASVARKHFLPdNQLKKIYQLSNILISEAFLLLRYLL 1447
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1688 KTFFTLAQLARNNARLD-IASESLMHCLERRLPQaelefaeilwkQGENDRALKIVQEIHEKYQENSSVNARDRAAVLLK 1766
Cdd:COG5032  1448 LCRLGRRELKAGLNVWNlTNLELFSDIQESEFFE-----------WGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKK 1516
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1767 FTEWLDLSNNSASEQIIKQYQDIFQIDSKWDK--PYYSIGLYYSRLLERKKAEGYITN-GRFEYRAISYFLLAFEKNTAK 1843
Cdd:COG5032  1517 LNLFELLGSLLSAKDAAGSYYKNFHIFDLEISviPFIPQLLSSLSLLDLNSAQSLLSKiGKEHPQALVFTLRSAIESTAL 1596
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1844 VRENLPkvitfwLDIAAASISEAPGNRKEMLSKATEDICShvEEALQHcptYIWYFVLTQLLSRLLHSHQSsaqiimhIL 1923
Cdd:COG5032  1597 SKESVA------LSLENKSRTHDPSLVKEALELSDENIRI--AYPLLH---LLFEPILAQLLSRLSSENNK-------IS 1658
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1924 LSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLtkaLTRVCLQDVKSITSRSGKSLEKD 2003
Cdd:COG5032  1659 VALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISLLNL---SRKLYISVLRSIRKRLKRLLELR 1735
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2004 FKFdmnVAPSAMVVPvrKNLDIISPLESNSMrgyqpfRPVVSIIRFGSSYKVFSS-LKKPKQLNIIGSDGNIYGIMCK-K 2081
Cdd:COG5032  1736 LKK---VSPKLLLFH--AFLEIKLPGQYLLD------KPFVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKgG 1804
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2082 EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKS-LHD 2160
Cdd:COG5032  1805 DDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKkLAA 1884
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2161 RWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVL 2240
Cdd:COG5032  1885 RLDNLKLLLKDEFFTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVI 1964
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2241 HVDF-DCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD------RNMD 2313
Cdd:COG5032  1965 HIDFgFILFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDpliewrRLPC 2044
                        2170      2180      2190      2200      2210      2220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365009 2314 HS------IQKALKVLRNKIRGIDPQDGLVLSVAGQTETLIQEATSEDNLSKMYIGWLPFW 2368
Cdd:COG5032  2045 FReiqnneIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
2046-2315 1.05e-119

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


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 378.00  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKpKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSILSTKYeslkikyslkslhdrwqhtavdgklefymeqvdkfPPILYQWFLENFPDPINWFNARN 2204
Cdd:cd00892    81 ECGIIEWVPNTVTLRSILSTLY-----------------------------------PPVLHEWFLKNFPDPTAWYEARN 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2205 TYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKS 2284
Cdd:cd00892   126 NYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRT 205
                         250       260       270
                  ....*....|....*....|....*....|.
gi 398365009 2285 SEVTLALMRKNEVALMNVIETIMYDRNMDHS 2315
Cdd:cd00892   206 CEVTLRVLRENRETLMSVLETFVHDPLVEWS 236
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2077-2313 2.00e-80

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


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 265.32  E-value: 2.00e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2077 IMCKK-EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSL 2155
Cdd:smart00146    1 VIFKGgDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2156 kslhdRWQHTAVDGKLEFYMEQVDKFP-PILYQWFLENFPDP-INWFNARNTYARSYAVMAMVGHILGLGDRHCENILLD 2233
Cdd:smart00146   81 -----RSQTATRLKKLELFLEATGKFPdPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2234 iQTGKVLHVDFDCLFEKGKRLPVP-EIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDRNM 2312
Cdd:smart00146  156 -KTGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLP 234

                    .
gi 398365009   2313 D 2313
Cdd:smart00146  235 D 235
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2074-2316 6.16e-77

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 255.33  E-value: 6.16e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2074 IYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRslgINIYSVLSLREDCGILEMVPNVVTLRSILSTKYES-LKI 2151
Cdd:pfam00454    1 GYGGIYKvGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENgVPP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2152 KYSLKSLHDRWQHTavDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENIL 2231
Cdd:pfam00454   78 TAMVKILHSALNYP--KLKLEFESRISLPPKVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNIL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2232 LDIQTGKVLHVDF-DCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDR 2310
Cdd:pfam00454  156 VDKTTGKLFHIDFgLCLPDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235

                   ....*.
gi 398365009  2311 NMDHSI 2316
Cdd:pfam00454  236 LPDWSI 241
 
Name Accession Description Interval E-value
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
194-2368 0e+00

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1385.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  194 TFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQLKyISLVVDYVCNRTISTALDAPALVCCeqLKF 273
Cdd:COG5032     1 DRLAQIIYALPSLLKDCFTEILLRKSDVRSSLFDLLHVSFLDYKEKDER-LSNVNDLVRNSTQSLLNTISNLIKI--VKF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  274 VLTTMHHFLDNKYGLLdNDPTMAKgILRLYSLCISNDFSKCFVDhfpidqwadfsQSEHFPFTQLTNKALSiVYFDLKRR 353
Cdd:COG5032    78 VLPLKSFFLSPIFAKL-RALPMTK-ILCISADTYCLSLSIKALA-----------DDESLTTILKTIRELL-SKFLLRLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  354 SLPVEALKYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQLSPGFFQRAGNDFK 433
Cdd:COG5032   144 LLFLFIGLLAQKFSEAQSKLFFKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNISDGNYFKVEIGRKL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  434 LILNEASVSIQTCFKTNNITR-LTSWTVILGRLACLESEKFSGTLPNSTKDMDNWYVCH-LCDIEKTGN-----PFVRIN 506
Cdd:COG5032   224 LDHLNALGQILDCQKIAKITKsFRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHfETDLFKTFLvtscfLFFVDE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  507 PNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLLSgILFSLHRIFSHF--QPPKLTDGNGQIN-KSFKLVQKCFMNSNRY 583
Cdd:COG5032   304 ICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRIS-ALSSLLVIFDYHlaLPDAVRLLFGESNdKVFLISELALDSTGRL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  584 LRLLSTRIIP-LFNISDSHNSEDEHTATLIKFLQSQKLpvvKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDySLR 662
Cdd:COG5032   383 LRVLPARVLPsLFEFLLSLLTVLKISGLILEFEISAQL---LCNLIRSSNQLLTSLISPYFLFILPKCIDSSNSEI-SYR 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  663 IMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTILDIFQRYIIPYAIIQYKSDVLS 742
Cdd:COG5032   459 VENLGELKDILGLDRITDYQALSLRLIIVSIQLRSFVFKREAINQIFKQLASIVIKPFLDYPKRLDLPIKIVTVVYVALL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  743 EIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHGLfsldiLETLFLNRAPTFDKGYITAYLPdykTLAEITKLYKN 822
Cdd:COG5032   539 RRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-----QLLAVYGFIRSIDDLYFTVSDP---TLIEILKLPVL 610
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  823 SVTKDAsDSENANMILCSLRFLITNFEKDKrHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTYYE 902
Cdd:COG5032   611 SIVHSA-IIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNFLELIVIAFFPLIRSEIIGIVLISSLFS 688
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  903 KLrvINGISFLIIyapkkSIISALAQIsiclqTGLGLKEVRYEAFRCWHLLVRHLNDEELSTVIDSLIafiLQKWSEFNG 982
Cdd:COG5032   689 KT--WILLKLLLI-----AFISKLISA-----LQGELKMLAPTLFTLFLVLVERYLDVEYSSVSFKLL---LVILVYFGG 753
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  983 KLRNIVYSILDtlikeksdLILKLKPYTTLalvGKPELGILARDGQFARMVNKIRSTTDLIPIFANNLKSSnKYVINQNL 1062
Cdd:COG5032   754 NLESLVLLILD--------LIVMLVEYTEL---GLQESIFIERLSQFFKFKNLSENASRLLPPLMDNLSKS-HELRCVSE 821
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1063 DDIEVYLRRKQTERSIDFTPkkvgqtsDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVT-KHEFKRTTYSEN 1141
Cdd:COG5032   822 DDVSALLIQLLTDRVICFIP-------VINSSLGDSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTdLREFFQTVKSKA 894
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1142 EVYDLNDSVQTIKFLIWVINDILVPAFWQSENpsKQLFVALVIQE---SLKYCGLSSESWDMNHKELY-PNEAKLWEKF- 1216
Cdd:COG5032   895 EVLSMLPFVQSILFEAWNRVDFLLKDFWQEEL--DNLLVALLKELpfmALRDCSILSDLYFMLGRELWnSVSFECWLELm 972
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1217 NSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKRFTLDLLKTGTtENHPLHVFSSLIREDDGSLSNFLlP 1296
Cdd:COG5032   973 NSYKRLLIKSLKSKLHLPTIPILILQMLLDSKNLTEFTEHQLKNLPLPSLSIGF-YESLCSFLAKLLHDEELYFFPLL-F 1050
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1297 YISLDIIIKAEKGTPYADILNGIIIEFDSIFTCNLEGMnnlQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFII 1376
Cdd:COG5032  1051 VSSLETLLSVNYHINQLDLRPNILKHFGSFVRFQLKPH---LVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDAL 1127
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1377 KDTKTTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQITYEEIGDIDSLDGVLR 1456
Cdd:COG5032  1128 GKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPFSLQYLYWHINDIDCADKLQS 1207
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1457 TFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRMLKSMYDHQ--LYSQIISNSSFHSSDGKISLSPDVKEW 1534
Cdd:COG5032  1208 VLAELSLVTGISELLLEESWRRALFSNIKDSLESELEEIIDGMYKSNEDFGalMLLSLSAELWDKILEGRSSCSKSIKLS 1287
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1535 YSIGLEAANLEGNVQTLKNWVEQIESLRNIDDREVLLQYNIAKALIAIS-NEDPLRTQKYI---HNSFRLIGTNFITSSK 1610
Cdd:COG5032  1288 LNIWLDLSIVVSPKDEPELFIKFVELCEASSIRSKLLEKNIQELLEKLEeIKSPLGTLRDRlppPWALLDLKRLLATWRQ 1367
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1611 ETTLLKKQNLLMKLHSLYDL--SFLSSAKDKFEYKSNTTILDYRMERIGADFVP-NHYILSMRKSFDQLKMNEQADADLG 1687
Cdd:COG5032  1368 NAFLRINPELLPLLSSLLNLqsSSLSKQLVSRGSSESAISINSFASVARKHFLPdNQLKKIYQLSNILISEAFLLLRYLL 1447
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1688 KTFFTLAQLARNNARLD-IASESLMHCLERRLPQaelefaeilwkQGENDRALKIVQEIHEKYQENSSVNARDRAAVLLK 1766
Cdd:COG5032  1448 LCRLGRRELKAGLNVWNlTNLELFSDIQESEFFE-----------WGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKK 1516
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1767 FTEWLDLSNNSASEQIIKQYQDIFQIDSKWDK--PYYSIGLYYSRLLERKKAEGYITN-GRFEYRAISYFLLAFEKNTAK 1843
Cdd:COG5032  1517 LNLFELLGSLLSAKDAAGSYYKNFHIFDLEISviPFIPQLLSSLSLLDLNSAQSLLSKiGKEHPQALVFTLRSAIESTAL 1596
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1844 VRENLPkvitfwLDIAAASISEAPGNRKEMLSKATEDICShvEEALQHcptYIWYFVLTQLLSRLLHSHQSsaqiimhIL 1923
Cdd:COG5032  1597 SKESVA------LSLENKSRTHDPSLVKEALELSDENIRI--AYPLLH---LLFEPILAQLLSRLSSENNK-------IS 1658
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1924 LSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLtkaLTRVCLQDVKSITSRSGKSLEKD 2003
Cdd:COG5032  1659 VALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISLLNL---SRKLYISVLRSIRKRLKRLLELR 1735
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2004 FKFdmnVAPSAMVVPvrKNLDIISPLESNSMrgyqpfRPVVSIIRFGSSYKVFSS-LKKPKQLNIIGSDGNIYGIMCK-K 2081
Cdd:COG5032  1736 LKK---VSPKLLLFH--AFLEIKLPGQYLLD------KPFVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKgG 1804
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2082 EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKS-LHD 2160
Cdd:COG5032  1805 DDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKkLAA 1884
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2161 RWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVL 2240
Cdd:COG5032  1885 RLDNLKLLLKDEFFTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVI 1964
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2241 HVDF-DCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD------RNMD 2313
Cdd:COG5032  1965 HIDFgFILFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDpliewrRLPC 2044
                        2170      2180      2190      2200      2210      2220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365009 2314 HS------IQKALKVLRNKIRGIDPQDGLVLSVAGQTETLIQEATSEDNLSKMYIGWLPFW 2368
Cdd:COG5032  2045 FReiqnneIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
2046-2315 1.05e-119

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


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 378.00  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKpKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSILSTKYeslkikyslkslhdrwqhtavdgklefymeqvdkfPPILYQWFLENFPDPINWFNARN 2204
Cdd:cd00892    81 ECGIIEWVPNTVTLRSILSTLY-----------------------------------PPVLHEWFLKNFPDPTAWYEARN 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2205 TYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKS 2284
Cdd:cd00892   126 NYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRT 205
                         250       260       270
                  ....*....|....*....|....*....|.
gi 398365009 2285 SEVTLALMRKNEVALMNVIETIMYDRNMDHS 2315
Cdd:cd00892   206 CEVTLRVLRENRETLMSVLETFVHDPLVEWS 236
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
2046-2309 3.68e-81

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


Pssm-ID: 270715 [Multi-domain]  Cd Length: 282  Bit Score: 269.41  E-value: 3.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd05171     1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKgGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRIRTYKVVPLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSIL--STKYESLKIKY---SLKSLHDRW-----QHTAVDGKLEFYMEQVDKFPPILYQWFLENFP 2194
Cdd:cd05171    81 RSGVLEFVENTIPLGEYLvgASSKSGAHARYrpkDWTASTCRKkmrekAKASAEERLKVFDEICKNFKPVFRHFFLEKFP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2195 DPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGI 2274
Cdd:cd05171   161 DPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGKLLPIPETVPFRLTRDIVDGMGI 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 398365009 2275 IGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD 2309
Cdd:cd05171   241 TGVEGVFRRCCEETLRVLRENKEALLTILEVLLYD 275
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2077-2313 2.00e-80

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


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 265.32  E-value: 2.00e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2077 IMCKK-EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSL 2155
Cdd:smart00146    1 VIFKGgDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2156 kslhdRWQHTAVDGKLEFYMEQVDKFP-PILYQWFLENFPDP-INWFNARNTYARSYAVMAMVGHILGLGDRHCENILLD 2233
Cdd:smart00146   81 -----RSQTATRLKKLELFLEATGKFPdPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   2234 iQTGKVLHVDFDCLFEKGKRLPVP-EIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDRNM 2312
Cdd:smart00146  156 -KTGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLP 234

                    .
gi 398365009   2313 D 2313
Cdd:smart00146  235 D 235
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2074-2316 6.16e-77

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 255.33  E-value: 6.16e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2074 IYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRslgINIYSVLSLREDCGILEMVPNVVTLRSILSTKYES-LKI 2151
Cdd:pfam00454    1 GYGGIYKvGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENgVPP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2152 KYSLKSLHDRWQHTavDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENIL 2231
Cdd:pfam00454   78 TAMVKILHSALNYP--KLKLEFESRISLPPKVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNIL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  2232 LDIQTGKVLHVDF-DCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDR 2310
Cdd:pfam00454  156 VDKTTGKLFHIDFgLCLPDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235

                   ....*.
gi 398365009  2311 NMDHSI 2316
Cdd:pfam00454  236 LPDWSI 241
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
2046-2309 2.68e-76

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


Pssm-ID: 270708 [Multi-domain]  Cd Length: 222  Bit Score: 252.96  E-value: 2.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCKK-EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd05164     1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGdDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRsilstkyeslkikyslkslhdrwqhtavdgklefymeqvdkfpPILYQWFLENFPDPINWFNARN 2204
Cdd:cd05164    81 QSGLIEWVDNTTTLK-------------------------------------------PVLKKWFNETFPDPTQWYEARS 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2205 TYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKS 2284
Cdd:cd05164   118 NYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIINGMGPTGVEGLFRKS 197
                         250       260
                  ....*....|....*....|....*
gi 398365009 2285 SEVTLALMRKNEVALMNVIETIMYD 2309
Cdd:cd05164   198 CEQVLRVFRKHKDKLITFLDTFLYD 222
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2046-2309 9.84e-58

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


Pssm-ID: 270714  Cd Length: 304  Bit Score: 202.87  E-value: 9.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKgLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSILSTKYES---------------------------LKIKYSLKS-----LHDRwQHTAVDGKLE 2172
Cdd:cd05170    81 RSGLIQWVDGATPLFSLYKRWQQRraaaqaqknqdsgstpppvprpselfyNKLKPALKAagirkSTSR-REWPLEVLRQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2173 FYMEQVDKFPP-ILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKG 2251
Cdd:cd05170   160 VLEELVAETPRdLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFEKG 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 398365009 2252 KRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD 2309
Cdd:cd05170   240 KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYD 297
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
2046-2309 7.01e-57

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


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 199.25  E-value: 7.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKgHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSILSTKYESLKI------KYSLKSLHDrWQHTAVDGKLEFYMEQVDKFPPI-LYQWFLENFPDPI 2197
Cdd:cd05169    81 NSGLIGWVPGCDTLHSLIRDYREKRKIplniehRLMLQMAPD-YDNLTLIQKVEVFEYALENTPGDdLRRVLWLKSPSSE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2198 NWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDF-DClFEKGK-RLPVPEIVPFRLTPNLLDALGII 2275
Cdd:cd05169   160 AWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFgDC-FEVAMhREKFPEKVPFRLTRMLVNAMEVS 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 398365009 2276 GTEGTFKKSSEVTLALMRKNEVALMNVIETIMYD 2309
Cdd:cd05169   239 GVEGTFRSTCEDVMRVLRENKDSLMAVLEAFVHD 272
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
2046-2314 1.02e-48

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


Pssm-ID: 270716 [Multi-domain]  Cd Length: 235  Bit Score: 174.30  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2046 IIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCK-KEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLRE 2124
Cdd:cd05172     1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKgGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2125 DCGILEMVPNVVTLRSILSTkyeslkikyslkslhdrwqhtavdgklefymeqvdkfpPILYQWFLENFPDPINWFNARN 2204
Cdd:cd05172    81 RLGLIEWVDNTTPLKEILEN--------------------------------------DLLRRALLSLASSPEAFLALRS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2205 TYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKR-LPVPEIVPFRLTPNLLDALGIIGTEGTFKK 2283
Cdd:cd05172   123 NFARSLAAMSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFGSATQfLPIPELVPFRLTRQLLNLLQPLDARGLLRS 202
                         250       260       270
                  ....*....|....*....|....*....|.
gi 398365009 2284 SSEVTLALMRKNEVALMNVIETIMYDRNMDH 2314
Cdd:cd05172   203 DMVHVLRALRAGRDLLLATMDVFVKEPLLDW 233
UME smart00802
Domain in UVSB PI-3 kinase, MEI-41 and ESR-1; Characteristic domain in UVSP PI-3 kinase, ...
872-979 1.48e-37

Domain in UVSB PI-3 kinase, MEI-41 and ESR-1; Characteristic domain in UVSP PI-3 kinase, MEI-41 and ESR-1. Found in nucleolar proteins. Associated with FAT, FATC, PI3_PI4_kinase modules.


Pssm-ID: 214825  Cd Length: 107  Bit Score: 137.34  E-value: 1.48e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009    872 FQKKLQDNILGIFQVFSSDIHDVEGRTTYYEKLRVINGISFLIIyAPKKSIISALAQISICLQTGLGLKEVRYEAFRCWH 951
Cdd:smart00802    1 LADFLKDHFLGILAVFSNILHDSSGKKPYNEKKRALRSIGFLIK-LMGKHISSALPQIMACLQSALEIPELRSLALRCWH 79
                            90       100
                    ....*....|....*....|....*...
gi 398365009    952 LLVRHLNDEELSTVIDSLIAFILQKWSE 979
Cdd:smart00802   80 VLIKTLKEEELGPLLDQIFAAILPLWPT 107
UME pfam08064
UME (NUC010) domain; This domain is characteriztic of UVSB PI-3 kinase, MEI-41 and ESR1.
876-977 3.65e-37

UME (NUC010) domain; This domain is characteriztic of UVSB PI-3 kinase, MEI-41 and ESR1.


Pssm-ID: 462350  Cd Length: 102  Bit Score: 136.08  E-value: 3.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009   876 LQDNILGIFQVFSSDIHDVEGRTTYYEKLRVINGISFLIIYApKKSIISALAQISICLQTGLGLKEVRYEAFRCWHLLVR 955
Cdd:pfam08064    2 LENHILGILARFSDVLNDLRGKKPVEEKKRALRSIEELIKLM-GSAISSALPQIMACLQSALEIPELREVALSCWDAFVK 80
                           90       100
                   ....*....|....*....|..
gi 398365009   956 HLNDEELSTVIDSLIAFILQKW 977
Cdd:pfam08064   81 TLDEEDLGPLLDQTFAAILQLW 102
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
2054-2309 7.66e-33

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


Pssm-ID: 270621 [Multi-domain]  Cd Length: 216  Bit Score: 127.83  E-value: 7.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSDGNIYGIMCKKED-VRQDNQYMQFATTMDFLLSKDiasrKRSLGINIYSVLSLREDCGILEMV 2132
Cdd:cd00142     9 KVIHSKQRPKKITLIGADGKTYSFLLKRRDdLRKDERSFQFMRLIQSILEKE----SVNLVLPPYKVIPLSENSGLIEIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2133 PNVVTLrsilstkyeslkikyslkslHDrwqhtavdgklefymeqvdkfppiLYQWFLENFPDPINWFNARNTYARSYAV 2212
Cdd:cd00142    85 KDAQTI--------------------ED------------------------LLKSLWRKSPSSQSWLNRRENFSCSLAG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2213 MAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALM 2292
Cdd:cd00142   121 YSVLGYIFGIGDRHPSNIMIE-PSGNIFHIDFGFIFSGRKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMVKIMEIL 199
                         250
                  ....*....|....*..
gi 398365009 2293 RKNEVALMNVIETIMYD 2309
Cdd:cd00142   200 REHADLIVPILEHSLRD 216
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
2040-2281 4.86e-20

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


Pssm-ID: 270707  Cd Length: 252  Bit Score: 91.81  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2040 FRPVVSIIR-FGSSYKvfsslkkpkQLNIIGSDGNIYGIMCKK---EDVRQDNQYMQFATTMDFLLSKDIASRKRSLGIN 2115
Cdd:cd05163     4 FLPRVEIVRrHGTCYR---------RLTIRGHDGSKYPFLVQTpsaRHSRREERVMQLFRLLNRVLERKKETRRRNLQFH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2116 iysvlslredcgilemVPNVVTLrsilSTKYESLKIKYSLKSLHDRWQhtavdgKLEFYMEQVDKFPP--ILYQWFLENF 2193
Cdd:cd05163    75 ----------------VPIVVPL----SPQVRLVEDDPSYISLQDIYE------KLEILNEIQSKMVPetILSNYFLRTM 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2194 PDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVlhVDFDCLFE---KGKRLPVPEIVPFRLTPNLLD 2270
Cdd:cd05163   129 PSPSDLWLFRKQFTLQLALSSFMTYVLSLGNRTPHRILISRSTGNV--FMTDFLPSinsQGPLLDNNEPVPFRLTPNIQH 206
                         250
                  ....*....|.
gi 398365009 2271 ALGIIGTEGTF 2281
Cdd:cd05163   207 FIGPIGVEGLL 217
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2054-2328 1.05e-16

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


Pssm-ID: 270628 [Multi-domain]  Cd Length: 346  Bit Score: 84.12  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSDGNIYGIMCKK-EDVRQDNQYMQFATTMDFLLskdiasRKRSLGINI--YSVLSLREDCGILE 2130
Cdd:cd00896    72 TVFKSALMPLKLTFKTLDGGEYKVIFKHgDDLRQDQLVLQIITLMDRLL------KKENLDLKLtpYKVLATSPNDGLVE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2131 MVPNVVTLRSILStkyeslkiKYslKSLHDRWQHTAVDGKLEFYMEqvdkfppilyqwflenfpdpinwFNARNTYARSY 2210
Cdd:cd00896   146 FVPNSKALADILK--------KY--GSILNFLRKHNPDESGPYGIK-----------------------PEVMDNFVKSC 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2211 AVMAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCLFekGkRLPVPEIVPFRLTPNLLDALGIIGTEGT--FKK-SSEV 2287
Cdd:cd00896   193 AGYCVITYILGVGDRHLDNLLLT-KDGHLFHIDFGYIL--G-RDPKPFPPPMKLCKEMVEAMGGANSEGYkeFKKyCCTA 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 398365009 2288 TLALmRKNEVALMNVIEtIMYD---RNMDHSIQKALKVLRNKIR 2328
Cdd:cd00896   269 YNIL-RKHANLILNLFS-LMVDaniPDIALEPDKAVLKVQEKFR 310
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2054-2273 7.17e-15

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


Pssm-ID: 270624 [Multi-domain]  Cd Length: 334  Bit Score: 78.38  E-value: 7.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD--GNIYGIMCKK-EDVRQDNQYMQFATTMDFLLSK---DiasrkrsLGINIYSVLSLREDCG 2127
Cdd:cd00891    65 KVMDSKKLPLWLVFKNADpgGDPIKVIFKAgDDLRQDQLTLQLLRIMDKLWKKeglD-------LRMTPYKCIATGDEVG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2128 ILEMVPNVVTLRSIlSTKYESLKIKYSLKSLHDrwqhtavdgklefymeqvdkfppilyqWFLENFPDPINWFNARNTYA 2207
Cdd:cd00891   138 MIEVVPNSETTAAI-QKKYGGFGAAFKDTPISN---------------------------WLKKHNPTEEEYEEAVENFI 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365009 2208 RSYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCL---FEK---GKRlpvpEIVPFRLTPNLLDALG 2273
Cdd:cd00891   190 RSCAGYCVATYVLGIGDRHNDNIMVT-KSGHLFHIDFGHFlgnFKKkfgIKR----ERAPFVFTPEMAYVMG 256
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
2082-2328 3.82e-13

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


Pssm-ID: 270626 [Multi-domain]  Cd Length: 286  Bit Score: 72.29  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2082 EDVRQDNQYMQFATTMDFLLskdiasRKRSLGI--NIYSVLSLREDCGILEMVPNVVTLRSilstkyeslkIKYSLKSLh 2159
Cdd:cd00893    36 DDLKQEQLALQLISQFDQIF------KEEGLPLwlRPYEILSLGPDSGIIEMIKNAVSIDS----------LKKKLDSF- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2160 DRWQHtavdgklefymeqvdkfppiLYQWFLENFPDPiNWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQtGKV 2239
Cdd:cd00893    99 NKFVS--------------------LSDFFDDNFGDE-AIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDKE-GHI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2240 LHVDFDCLFE-KGKRLPVpEIVPFRLTPNLLDALGIIGTE--GTFKKSSEVTLALMRKNEVALMNVIEtIMYDRNMDHSI 2316
Cdd:cd00893   157 IHIDFGFFLSsHPGFYGF-EGAPFKLSSEYIEVLGGVDSElfKEFRKLFLKGFMALRKHSDKILSLVE-MMYSGHGITCF 234
                         250
                  ....*....|...
gi 398365009 2317 -QKALKVLRNKIR 2328
Cdd:cd00893   235 gKKTIQQLKQRFN 247
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2054-2244 5.10e-13

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


Pssm-ID: 270710 [Multi-domain]  Cd Length: 352  Bit Score: 73.09  E-value: 5.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD---GNIYgIMCKK-EDVRQDNQYMQFATTMDFLLSKDiasrKRSLGINIYSVLSLREDCGIL 2129
Cdd:cd05166    68 SYFNSNALPLKLVFRNADpraEPIS-VIFKVgDDLRQDMLTLQLIRIMDKIWLQE----GLDLKMITFRCVPTGNKRGMV 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2130 EMVPNVVTLRSIlstkyeslKIKYSLK-SLHDRwqhtavdgklefymeqvdkfppILYQWFLENFPDPINWFNARNTYAR 2208
Cdd:cd05166   143 ELVPEAETLREI--------QTEHGLTgSFKDR----------------------PLADWLQKHNPSELEYEKAVENFIR 192
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 398365009 2209 SYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDF 2244
Cdd:cd05166   193 SCAGYCVATYVLGICDRHNDNIMLK-TSGHLFHIDF 227
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
2338-2368 2.08e-12

FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution structure of the FATC domain suggests it plays a role in redox-dependent structural and cellular stability.


Pssm-ID: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 63.17  E-value: 2.08e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 398365009  2338 LSVAGQTETLIQEATSEDNLSKMYIGWLPFW 2368
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPWW 32
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
2083-2273 2.06e-09

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


Pssm-ID: 270711 [Multi-domain]  Cd Length: 307  Bit Score: 61.46  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2083 DVRQDNQYMQFATtmdflLSKDIAsrkRSLGINI----YSVLSLREDCGILEMVPNVvtlrsilstkyeslkikyslKSL 2158
Cdd:cd05167    59 DCRQDMLALQLIS-----LFKNIF---EEVGLDLylfpYRVVATGPGCGVIEVIPNS--------------------KSR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2159 HDRWQHTAVDgklefymeqvdkfppiLYQWFLENFPDP--INWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQt 2236
Cdd:cd05167   111 DQIGRETDNG----------------LYEYFLSKYGDEstPAFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDD- 173
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 398365009 2237 GKVLHVDFDCLFE--KGKRLPVpEIVPFRLTPNLLDALG 2273
Cdd:cd05167   174 GHIIHIDFGFIFEisPGGNLGF-ESAPFKLTKEMVDLMG 211
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2054-2285 5.06e-09

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


Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 60.65  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD-----GNIYGIMCKK-EDVRQDNQYMQFATTMDFLLskdiasRKRSLGINI--YSVLSLRED 2125
Cdd:cd00894    74 KVMASKKKPLWLEFKCADptalsNETIGIIFKHgDDLRQDMLILQILRIMESIW------ETESLDLCLlpYGCISTGDK 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2126 CGILEMVPNVVTLRSIlstkyeslkikyslkslhdrwQHTAVDGKLEFYMEqvdkfppILYQWFLENFPDPINWFNARNT 2205
Cdd:cd00894   148 IGMIEIVKDATTIAKI---------------------QQSTVGNTGAFKDE-------VLNHWLKEKCPIEEKFQAAVER 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2206 YARSYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCLFEKGKRL--PVPEIVPFRLTPNLLDALGIIGtegtfKK 2283
Cdd:cd00894   200 FVYSCAGYCVATFVLGIGDRHNDNIMIT-ETGNLFHIDFGHILGNYKSFlgINKERVPFVLTPDFLFVMGTSG-----KK 273

                  ..
gi 398365009 2284 SS 2285
Cdd:cd00894   274 TS 275
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2054-2286 5.27e-09

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


Pssm-ID: 270709 [Multi-domain]  Cd Length: 363  Bit Score: 60.73  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD-----GNIYGIMCKK-EDVRQDNQYMQFATTMDFLLSKDiasrKRSLGINIYSVLSLREDCG 2127
Cdd:cd05165    70 KVMDSKKRPLWLVFENADplalsGEDIKIIFKNgDDLRQDMLTLQIIRIMDNIWKEE----GLDLRMLPYGCLSTGDNVG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2128 ILEMVPNVVTLRSILSTKYESLKIKYSLKSLHDrwqhtavdgklefymeqvdkfppilyqWFLENFPDPINWFNARNTYA 2207
Cdd:cd05165   146 LIEVVRNAKTIANIQKKKGKVATLAFNKDSLHK---------------------------WLKEKNKTGEKYDRAIEEFT 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2208 RSYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCL---FEKG---KRlpvpEIVPFRLTPnllDALGIIGTEGTF 2281
Cdd:cd05165   199 LSCAGYCVATYVLGIGDRHSDNIMVK-ENGQLFHIDFGHFlgnFKKKfgiKR----ERVPFVLTH---DFVYVIARGQDN 270

                  ....*
gi 398365009 2282 KKSSE 2286
Cdd:cd05165   271 TKSEE 275
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
1664-1853 8.89e-07

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 53.51  E-value: 8.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  1664 HYILSMRKSFDQLKMNEQADADLGKTFFTLAQLARNNARLDIASESLMHCLERR----LPQAELEFAEILWKQGENDRAL 1739
Cdd:pfam02259  126 QDILTVRSLVLSPIEDVYLGGYHAEMWLKFANLARKSGRFSLAEKALLKLLGEDpeewLPEVVYAYAKYLWPTGEQQEAL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009  1740 -KIVQEIHEKYQENSSVN--------------ARDRAAVLLKFTEWLDLSNNSASEQ----IIKQYQDIFQIDSKWDKPY 1800
Cdd:pfam02259  206 lKLREFLSCYLQKNGELLsglevinptnleefTELLARCYLLKGKWQAALGQNWAEEkseeILQAYLLATQFDPSWYKAW 285
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 398365009  1801 YSIGLYY----SRLLERKKAEGYITNGRFEYRAISYFLLAFEKNTAKVRENLPKVIT 1853
Cdd:pfam02259  286 HTWALFNfevlRKEEQGKEEEGPEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
2117-2273 2.79e-06

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


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 51.71  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2117 YSVLSLREDCGILEMVPNVVTLRSIlstkyeslkikyslKSlhdrwqhtavdgklefymeqvdKFPPI--LYQWFLENF- 2193
Cdd:cd05168    70 YEILVTSSDSGLIETIPDTVSIDSL--------------KK----------------------RFPNFtsLLDYFERTFg 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2194 -PDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQtGKVLHVDFDCL---------FEKgkrlpvpeiVPFR 2263
Cdd:cd05168   114 dPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSE-GHIIHIDFGFMlsnspgglgFET---------APFK 183
                         170
                  ....*....|
gi 398365009 2264 LTPNLLDALG 2273
Cdd:cd05168   184 LTQEYVEVMG 193
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2054-2244 3.11e-06

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


Pssm-ID: 270721 [Multi-domain]  Cd Length: 354  Bit Score: 51.82  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD---GNIyGIMCKK-EDVRQDNQYMQFATTMDFLLSKDiasrKRSLGINIYSVLSLREDCGIL 2129
Cdd:cd05177    69 SYFTSNAAPLKISFINANplaKNI-SIIFKTgDDLRQDMLVLQIVRVMDNIWLQE----GLDMQMIIYRCLSTGKTQGLV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2130 EMVPNVVTLRSIL--STKYESLKiKYSLKSLHDRWQHTAVDgklefymeqvdkfppilYQWFLENFpdpinwfnarntyA 2207
Cdd:cd05177   144 QMVPDAVTLAKIHreSGLIGPLK-ENTIEKWFHMHNKLKED-----------------YDKAVRNF-------------F 192
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 398365009 2208 RSYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDF 2244
Cdd:cd05177   193 HSCAGWCVVTFILGVCDRHNDNIMLT-HSGHMFHIDF 228
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2072-2295 5.08e-04

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


Pssm-ID: 270717 [Multi-domain]  Cd Length: 362  Bit Score: 44.95  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2072 GNIYGIMCKK-EDVRQDNQYMQFATTMDFLLskdiasRKRSLGINI--YSVLSLREDCGILEMVPNVVTLRSIlstkyes 2148
Cdd:cd05173    92 GDSLGIIFKNgDDLRQDMLTLQILRLMDTLW------KEAGLDLRIvpYGCLATGDRSGLIEVVSSAETIADI------- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2149 lkikySLKSlhdrwqhTAVDGKLEFYMEQvdkfppiLYQWFLE-NFPDPINwfNARNTYARSYAVMAMVGHILGLGDRHC 2227
Cdd:cd05173   159 -----QLNS-------SNVAAAAAFNKDA-------LLNWLKEyNSGDDLE--RAIEEFTLSCAGYCVATYVLGIGDRHS 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365009 2228 ENILLDiQTGKVLHVDFDCLFE--KGKRLPVPEIVPFRLTPNLLDAL--GIIG-TE--GTFKKSSEVTLALMRKN 2295
Cdd:cd05173   218 DNIMVR-KNGQLFHIDFGHILGnfKSKFGIKRERVPFILTYDFIHVIqqGKTGnTEkfGRFRQYCEDAYLILRKN 291
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
1690-1908 6.41e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.95  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1690 FFTLAQLARNNARLDIASESLMHCLER--RLPQAELEFAEILWKQGENDRALKIVQEIHEKYQENSSVNAR--------- 1758
Cdd:COG2956    11 WYFKGLNYLLNGQPDKAIDLLEEALELdpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLElaqdylkag 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1759 --DRAAVLLKFTEWLDLSNNSASEQIIkqyqDIFQIDSKWDKpyySIgLYYSRLLERK---------KAEGYITNGRFEy 1827
Cdd:COG2956    91 llDRAEELLEKLLELDPDDAEALRLLA----EIYEQEGDWEK---AI-EVLERLLKLGpenahayceLAELYLEQGDYD- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 1828 RAISYFLLAFEKNTAKVR------------ENLPKVITFWLDIAAASISEAPGnrKEMLSKA------TEDICSHVEEAL 1889
Cdd:COG2956   162 EAIEALEKALKLDPDCARallllaelyleqGDYEEAIAALERALEQDPDYLPA--LPRLAELyeklgdPEEALELLRKAL 239
                         250
                  ....*....|....*....
gi 398365009 1890 QHCPTYIWYFVLTQLLSRL 1908
Cdd:COG2956   240 ELDPSDDLLLALADLLERK 258
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
2054-2269 1.59e-03

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


Pssm-ID: 270719 [Multi-domain]  Cd Length: 370  Bit Score: 43.12  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2054 KVFSSLKKPKQLNIIGSD-------GNIYGIMCKKEDVRQDNQYMQFATTMDFLLSkdiaSRKRSLGINIYSVLSLREDC 2126
Cdd:cd05175    76 RIMSSAKRPLWLNWENPDimsellfQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQ----NQGLDLRMLPYGCLSIGDCV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365009 2127 GILEMVPNVVTLRSIlstkyeslKIKYSLKslhdrwqhtavdGKLEFYMEQvdkfppiLYQWFLENFPDPInWFNARNTY 2206
Cdd:cd05175   152 GLIEVVRNSHTIMQI--------QCKGGLK------------GALQFNSHT-------LHQWLKDKNKGEI-YDAAIDLF 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365009 2207 ARSYAVMAMVGHILGLGDRHCENILLDiQTGKVLHVDFDCLFE-KGKRLPVP-EIVPFRLTPNLL 2269
Cdd:cd05175   204 TRSCAGYCVATFILGIGDRHNSNIMVK-DDGQLFHIDFGHFLDhKKKKFGYKrERVPFVLTQDFL 267
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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