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Conserved domains on  [gi|1019688|gb|AAB39292|]
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ORF YJR066w [Saccharomyces cerevisiae]

Protein Classification

HEAT_EZ and PIKKc_TOR domain-containing protein( domain architecture ID 12145833)

HEAT_EZ and PIKKc_TOR domain-containing protein

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];
279-2470 0e+00

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


:

Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1787.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   279 KCLSTLRNRDPQLTSQWVQRLATSCEYgFQVNTLECIHASLLVYKEILFlkdpFLNQVFDQMCLNCIAYENHKAKMIReK 358
Cdd:COG5032    1 DRLAQIIYALPSLLKDCFTEILLRKSD-VRSSLFDLLHVSFLDYKEKDE----RLSNVNDLVRNSTQSLLNTISNLIK-I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   359 IYQIVPLLASFNPQLFAgKYLHQIMDNYLEILTNAPANKIPHLkddkpqilisigdiayevGPDIAPYVKQILDYIeHDL 438
Cdd:COG5032   75 VKFVLPLKSFFLSPIFA-KLRALPMTKILCISADTYCLSLSIK------------------ALADDESLTTILKTI-REL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   439 QTKFKFRKKfenEIFYCIGRLAVPLGPVLGKLLnRNILDLMFKCPLSDYMQETFQILTERIPSLGPKINDELLNLVCSTL 518
Cdd:COG5032  135 LSKFLLRLR---LLFLFIGLLAQKFSEAQSKLF-FKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNIS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   519 SGTPFIQPGSPMEIPSFSRErAREWRNKNILQKTGEsnddNNDIKIIIQAFRMLKNIKSRFSLVEFVRIVALSYIEHTDP 598
Cdd:COG5032  211 DGNYFKVEIGRKLLDHLNAL-GQILDCQKIAKITKS----FRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHFET 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   599 RVRKLAALTSCEIYVKDNICKQTSLHSLNTVSEVLSKLLAITIADPLQDIRLEVLKNLNPCFDPQLAQPDNLRLLFTALH 678
Cdd:COG5032  286 DLFKTFLVTSCFLFFVDEICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRISALSSLLVIFDYHLALPDAVRLLFGESN 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   679 DESFNIQSVAMELVGRLSSVNPAYVIPSIRKILLELLTKLKFSTSSREKEETASLLCTLIRSSKDVAKPYIEPLLNVLLP 758
Cdd:COG5032  366 DKVFLISELALDSTGRLLRVLPARVLPSLFEFLLSLLTVLKISGLILEFEISAQLLCNLIRSSNQLLTSLISPYFLFILP 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   759 KFQDTSSTVASTALRTIGELSVVGGEDMKI-YLKDLFPLIIKTFQDQSNSFKREAALKALGQLAassGYVIDPLLDYPEL 837
Cdd:COG5032  446 KCIDSSNSEISYRVENLGELKDILGLDRITdYQALSLRLIIVSIQLRSFVFKREAINQIFKQLA---SIVIKPFLDYPKR 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   838 LGILVNILKTENSQNIRRQTVTLIGILGAIDPYRQKEREVTSTTDISTEQNAPPIdIALLMQGMSPSNDEYYTTVVIHCL 917
Cdd:COG5032  523 LDLPIKIVTVVYVALLRRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-QLLAVYGFIRSIDDLYFTVSDPTL 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   918 LKILKDPSLSSYHTAVIQAIMHIFQTLGLKCVSFLDQIiPTILDVMRTCSQSLLEFYFQQ-LCSLIIIVRQHIRPHVDSI 996
Cdd:COG5032  602 IEILKLPVLSIVHSAIIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNfLELIVIAFFPLIRSEIIGI 680
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   997 FQAIKDFSSV-AKLQITLVSVIEAISKALEGEFKRLVPLTLTLFLVILE--NDKSSDKVLSRRVLRLLESFGPNLEGYSH 1073
Cdd:COG5032  681 VLISSLFSKTwILLKLLLIAFISKLISALQGELKMLAPTLFTLFLVLVEryLDVEYSSVSFKLLLVILVYFGGNLESLVL 760
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1074 LITPKIVQMAEFTSGNLQRSAIIT-IGKLAKDVDLFEMSSRIVHSLLRVLSSttSDELSKVIMNTLSLLLIQMGTSFAI- 1151
Cdd:COG5032  761 LILDLIVMLVEYTELGLQESIFIErLSQFFKFKNLSENASRLLPPLMDNLSK--SHELRCVSEDDVSALLIQLLTDRVIc 838
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1152 FIPVINEVLM-KKHIQHTIYDDLTNRILNNDVLPTKILEANTTDYKPAEQMEAADAGVAK-LPINQSVLKSAWNSSQQRT 1229
Cdd:COG5032  839 FIPVINSSLGdSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTDLREFFQTVKSKAEVLSmLPFVQSILFEAWNRVDFLL 918
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1230 KEDWQEWSKRLSIQLLKESPSHALRACSNLASMYYPLAKELFNTAFACVWTELYSQYQEDLIGSLCIALSSPLNPPEIHQ 1309
Cdd:COG5032  919 KDFWQEELDNLLVALLKELPFMALRDCSILSDLYFMLGRELWNSVSFECWLELMNSYKRLLIKSLKSKLHLPTIPILILQ 998
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1310 TLL---NLVEFMEHDDKALPIPTQSLGEYAERCHAYAKALHYKEIKFIKEPENSTIESLISINNQLNQTDAAIGILKHAQ 1386
Cdd:COG5032  999 MLLdskNLTEFTEHQLKNLPLPSLSIGFYESLCSFLAKLLHDEELYFFPLLFVSSLETLLSVNYHINQLDLRPNILKHFG 1078
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1387 QHHSLQLKETWFEKLERWEDALHAYNEREKAGDTSVSVTLGKMRSLHALGEWEQLSQLAARKWKVSKLQTKKLIAPLAAG 1466
Cdd:COG5032 1079 SFVRFQLKPHLVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVAT 1158
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1467 AAWGLGEWDMLEQYISVMKPKSPDKEFFD--AILYLHKNDYDNASKHIL-NARDLLVTEISAL-INESYNRAYSVIVRTQ 1542
Cdd:COG5032 1159 AYEQVGEWYKAQQLYEVAQRKARSKEFPFslQYLYWHINDIDCADKLQSvLAELSLVTGISELlLEESWRRALFSNIKDS 1238
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1543 IITEFEEIIK--YKQLPPNSEK--KLHYQNLWTKRLLG---CQKNVDLWQRVLRVRSLVIKPKQDLQIWIKFANLCRKSG 1615
Cdd:COG5032 1239 LESELEEIIDgmYKSNEDFGALmlLSLSAELWDKILEGrssCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASS 1318
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1616 -RMRLANKALNMLLE-GGNDPSLPNTFKA--PPPVVYAQLKYIWATGAYKEALNHLIGFTSRLAHDLGLDPNNMIAQSVK 1691
Cdd:COG5032 1319 iRSKLLEKNIQELLEkLEEIKSPLGTLRDrlPPPWALLDLKRLLATWRQNAFLRINPELLPLLSSLLNLQSSSLSKQLVS 1398
                       1450      1460      1470      1480      1490      1500      1510      1520
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1692 LSSASTAPYVEEYTKLLARCFLKQGEWRIATQPNWRNTNPDAILGSYLLATHFDKNWYKAWHN-WALANFEVISMVQEET 1770
Cdd:COG5032 1399 RGSSESAISINSFASVARKHFLPDNQLKKIYQLSNILISEAFLLLRYLLLCRLGRRELKAGLNvWNLTNLELFSDIQESE 1478
                       1530      1540      1550      1560      1570      1580      1590      1600
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1771 KlnggkndddddtavnndnvridgsilgsgsltingNRYPLELIQRHVVPAIKGFFHSISLLETSCLQDTLRLLTLLFNF 1850
Cdd:COG5032 1479 F-----------------------------------FEWGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELL 1523
                       1610      1620      1630      1640      1650      1660      1670      1680
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1851 GGIKEVSQAMYEGFNLMKIE-NWLEVLPQLISRIHQPDPTVSNSLLSLLSDLGKAHPQALVYPLTVAIKSESVSRQKAAL 1929
Cdd:COG5032 1524 GSLLSAKDAAGSYYKNFHIFdLEISVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVAL 1603
                       1690      1700      1710      1720      1730      1740      1750      1760
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1930 SIIEKIRIHSPVLVNQAELVSHELIR-VAVLWHELWYEGLEDASRQFFVEHN-IEKMFSTLEPLHKHLGNEPQTLSEVSF 2007
Cdd:COG5032 1604 SLENKSRTHDPSLVKEALELSDENIRiAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSF 1683
                       1770      1780      1790      1800      1810      1820      1830      1840
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2008 QKSFGRDLNDAYEWLNNYKKSKDINNLNQAWDIYYNVFRKITRQIPQLQTLDLQHVSPQLLATHD-LELAVPGTYFPGKP 2086
Cdd:COG5032 1684 QSSFLKELIKKSPRKIRKKFKIDISLLNLSRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAfLEIKLPGQYLLDKP 1763
                       1850      1860      1870      1880      1890      1900      1910      1920
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2087 TIRIAKFEPLFSVISS-KQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAI 2165
Cdd:COG5032 1764 FVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVI 1843
                       1930      1940      1950      1960      1970      1980      1990      2000
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2166 PLSPKSGLLGWVPNSDTFHVLIREHRDAKKIPLNIEHwvmlQMAPDYENLTLLQKIEVFTYALDNTKgQDLYKILWLKSR 2245
Cdd:COG5032 1844 PLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEK----KLAARLDNLKLLLKDEFFTKATLKSP-PVLYDWFSESFP 1918
                       2010      2020      2030      2040      2050      2060      2070      2080
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2246 SSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAME 2325
Cdd:COG5032 1919 NPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFGFILFNAPGRFPFPEKVPFRLTRNIVEAMG 1998
                       2090      2100      2110      2120      2130      2140      2150      2160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2326 VSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHWGFdlppqklteqtgipLPLInpsellrkgaitveeaanm 2405
Cdd:COG5032 1999 VSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR--------------LPCF------------------- 2045
                       2170      2180      2190      2200      2210      2220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1019688  2406 eaeqqNETKNARAMLVLRRITDKLTGNDIKRFNELDVPEQVDKLIQQATSIERLCQHYIGWCPFW 2470
Cdd:COG5032 2046 -----REIQNNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
229-279 6.30e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


:

Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.96  E-value: 6.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1019688     229 KHAALLIITALAENCPYLLYQYLNSILDNIWRALRDPHLVIRIDASITLAK 279
Cdd:pfam13513    4 REAAALALGSLAEGGPDLLAPAVPELLPALLPLLNDDSDLVREAAAWALGR 54
 
Name Accession Description Interval E-value
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
279-2470 0e+00

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1787.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   279 KCLSTLRNRDPQLTSQWVQRLATSCEYgFQVNTLECIHASLLVYKEILFlkdpFLNQVFDQMCLNCIAYENHKAKMIReK 358
Cdd:COG5032    1 DRLAQIIYALPSLLKDCFTEILLRKSD-VRSSLFDLLHVSFLDYKEKDE----RLSNVNDLVRNSTQSLLNTISNLIK-I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   359 IYQIVPLLASFNPQLFAgKYLHQIMDNYLEILTNAPANKIPHLkddkpqilisigdiayevGPDIAPYVKQILDYIeHDL 438
Cdd:COG5032   75 VKFVLPLKSFFLSPIFA-KLRALPMTKILCISADTYCLSLSIK------------------ALADDESLTTILKTI-REL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   439 QTKFKFRKKfenEIFYCIGRLAVPLGPVLGKLLnRNILDLMFKCPLSDYMQETFQILTERIPSLGPKINDELLNLVCSTL 518
Cdd:COG5032  135 LSKFLLRLR---LLFLFIGLLAQKFSEAQSKLF-FKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNIS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   519 SGTPFIQPGSPMEIPSFSRErAREWRNKNILQKTGEsnddNNDIKIIIQAFRMLKNIKSRFSLVEFVRIVALSYIEHTDP 598
Cdd:COG5032  211 DGNYFKVEIGRKLLDHLNAL-GQILDCQKIAKITKS----FRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHFET 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   599 RVRKLAALTSCEIYVKDNICKQTSLHSLNTVSEVLSKLLAITIADPLQDIRLEVLKNLNPCFDPQLAQPDNLRLLFTALH 678
Cdd:COG5032  286 DLFKTFLVTSCFLFFVDEICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRISALSSLLVIFDYHLALPDAVRLLFGESN 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   679 DESFNIQSVAMELVGRLSSVNPAYVIPSIRKILLELLTKLKFSTSSREKEETASLLCTLIRSSKDVAKPYIEPLLNVLLP 758
Cdd:COG5032  366 DKVFLISELALDSTGRLLRVLPARVLPSLFEFLLSLLTVLKISGLILEFEISAQLLCNLIRSSNQLLTSLISPYFLFILP 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   759 KFQDTSSTVASTALRTIGELSVVGGEDMKI-YLKDLFPLIIKTFQDQSNSFKREAALKALGQLAassGYVIDPLLDYPEL 837
Cdd:COG5032  446 KCIDSSNSEISYRVENLGELKDILGLDRITdYQALSLRLIIVSIQLRSFVFKREAINQIFKQLA---SIVIKPFLDYPKR 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   838 LGILVNILKTENSQNIRRQTVTLIGILGAIDPYRQKEREVTSTTDISTEQNAPPIdIALLMQGMSPSNDEYYTTVVIHCL 917
Cdd:COG5032  523 LDLPIKIVTVVYVALLRRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-QLLAVYGFIRSIDDLYFTVSDPTL 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   918 LKILKDPSLSSYHTAVIQAIMHIFQTLGLKCVSFLDQIiPTILDVMRTCSQSLLEFYFQQ-LCSLIIIVRQHIRPHVDSI 996
Cdd:COG5032  602 IEILKLPVLSIVHSAIIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNfLELIVIAFFPLIRSEIIGI 680
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   997 FQAIKDFSSV-AKLQITLVSVIEAISKALEGEFKRLVPLTLTLFLVILE--NDKSSDKVLSRRVLRLLESFGPNLEGYSH 1073
Cdd:COG5032  681 VLISSLFSKTwILLKLLLIAFISKLISALQGELKMLAPTLFTLFLVLVEryLDVEYSSVSFKLLLVILVYFGGNLESLVL 760
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1074 LITPKIVQMAEFTSGNLQRSAIIT-IGKLAKDVDLFEMSSRIVHSLLRVLSSttSDELSKVIMNTLSLLLIQMGTSFAI- 1151
Cdd:COG5032  761 LILDLIVMLVEYTELGLQESIFIErLSQFFKFKNLSENASRLLPPLMDNLSK--SHELRCVSEDDVSALLIQLLTDRVIc 838
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1152 FIPVINEVLM-KKHIQHTIYDDLTNRILNNDVLPTKILEANTTDYKPAEQMEAADAGVAK-LPINQSVLKSAWNSSQQRT 1229
Cdd:COG5032  839 FIPVINSSLGdSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTDLREFFQTVKSKAEVLSmLPFVQSILFEAWNRVDFLL 918
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1230 KEDWQEWSKRLSIQLLKESPSHALRACSNLASMYYPLAKELFNTAFACVWTELYSQYQEDLIGSLCIALSSPLNPPEIHQ 1309
Cdd:COG5032  919 KDFWQEELDNLLVALLKELPFMALRDCSILSDLYFMLGRELWNSVSFECWLELMNSYKRLLIKSLKSKLHLPTIPILILQ 998
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1310 TLL---NLVEFMEHDDKALPIPTQSLGEYAERCHAYAKALHYKEIKFIKEPENSTIESLISINNQLNQTDAAIGILKHAQ 1386
Cdd:COG5032  999 MLLdskNLTEFTEHQLKNLPLPSLSIGFYESLCSFLAKLLHDEELYFFPLLFVSSLETLLSVNYHINQLDLRPNILKHFG 1078
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1387 QHHSLQLKETWFEKLERWEDALHAYNEREKAGDTSVSVTLGKMRSLHALGEWEQLSQLAARKWKVSKLQTKKLIAPLAAG 1466
Cdd:COG5032 1079 SFVRFQLKPHLVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVAT 1158
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1467 AAWGLGEWDMLEQYISVMKPKSPDKEFFD--AILYLHKNDYDNASKHIL-NARDLLVTEISAL-INESYNRAYSVIVRTQ 1542
Cdd:COG5032 1159 AYEQVGEWYKAQQLYEVAQRKARSKEFPFslQYLYWHINDIDCADKLQSvLAELSLVTGISELlLEESWRRALFSNIKDS 1238
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1543 IITEFEEIIK--YKQLPPNSEK--KLHYQNLWTKRLLG---CQKNVDLWQRVLRVRSLVIKPKQDLQIWIKFANLCRKSG 1615
Cdd:COG5032 1239 LESELEEIIDgmYKSNEDFGALmlLSLSAELWDKILEGrssCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASS 1318
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1616 -RMRLANKALNMLLE-GGNDPSLPNTFKA--PPPVVYAQLKYIWATGAYKEALNHLIGFTSRLAHDLGLDPNNMIAQSVK 1691
Cdd:COG5032 1319 iRSKLLEKNIQELLEkLEEIKSPLGTLRDrlPPPWALLDLKRLLATWRQNAFLRINPELLPLLSSLLNLQSSSLSKQLVS 1398
                       1450      1460      1470      1480      1490      1500      1510      1520
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1692 LSSASTAPYVEEYTKLLARCFLKQGEWRIATQPNWRNTNPDAILGSYLLATHFDKNWYKAWHN-WALANFEVISMVQEET 1770
Cdd:COG5032 1399 RGSSESAISINSFASVARKHFLPDNQLKKIYQLSNILISEAFLLLRYLLLCRLGRRELKAGLNvWNLTNLELFSDIQESE 1478
                       1530      1540      1550      1560      1570      1580      1590      1600
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1771 KlnggkndddddtavnndnvridgsilgsgsltingNRYPLELIQRHVVPAIKGFFHSISLLETSCLQDTLRLLTLLFNF 1850
Cdd:COG5032 1479 F-----------------------------------FEWGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELL 1523
                       1610      1620      1630      1640      1650      1660      1670      1680
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1851 GGIKEVSQAMYEGFNLMKIE-NWLEVLPQLISRIHQPDPTVSNSLLSLLSDLGKAHPQALVYPLTVAIKSESVSRQKAAL 1929
Cdd:COG5032 1524 GSLLSAKDAAGSYYKNFHIFdLEISVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVAL 1603
                       1690      1700      1710      1720      1730      1740      1750      1760
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1930 SIIEKIRIHSPVLVNQAELVSHELIR-VAVLWHELWYEGLEDASRQFFVEHN-IEKMFSTLEPLHKHLGNEPQTLSEVSF 2007
Cdd:COG5032 1604 SLENKSRTHDPSLVKEALELSDENIRiAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSF 1683
                       1770      1780      1790      1800      1810      1820      1830      1840
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2008 QKSFGRDLNDAYEWLNNYKKSKDINNLNQAWDIYYNVFRKITRQIPQLQTLDLQHVSPQLLATHD-LELAVPGTYFPGKP 2086
Cdd:COG5032 1684 QSSFLKELIKKSPRKIRKKFKIDISLLNLSRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAfLEIKLPGQYLLDKP 1763
                       1850      1860      1870      1880      1890      1900      1910      1920
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2087 TIRIAKFEPLFSVISS-KQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAI 2165
Cdd:COG5032 1764 FVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVI 1843
                       1930      1940      1950      1960      1970      1980      1990      2000
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2166 PLSPKSGLLGWVPNSDTFHVLIREHRDAKKIPLNIEHwvmlQMAPDYENLTLLQKIEVFTYALDNTKgQDLYKILWLKSR 2245
Cdd:COG5032 1844 PLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEK----KLAARLDNLKLLLKDEFFTKATLKSP-PVLYDWFSESFP 1918
                       2010      2020      2030      2040      2050      2060      2070      2080
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2246 SSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAME 2325
Cdd:COG5032 1919 NPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFGFILFNAPGRFPFPEKVPFRLTRNIVEAMG 1998
                       2090      2100      2110      2120      2130      2140      2150      2160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2326 VSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHWGFdlppqklteqtgipLPLInpsellrkgaitveeaanm 2405
Cdd:COG5032 1999 VSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR--------------LPCF------------------- 2045
                       2170      2180      2190      2200      2210      2220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1019688  2406 eaeqqNETKNARAMLVLRRITDKLTGNDIKRFNELDVPEQVDKLIQQATSIERLCQHYIGWCPFW 2470
Cdd:COG5032 2046 -----REIQNNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
2090-2366 0e+00

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: 570.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05169    1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTFHVLIREHRDAKKIPLNIEHWVMLQMAPDYENLTLLQKIEVFTYALDNTKGQDLYKILWLKSRSSET 2249
Cdd:cd05169   81 NSGLIGWVPGCDTLHSLIRDYREKRKIPLNIEHRLMLQMAPDYDNLTLIQKVEVFEYALENTPGDDLRRVLWLKSPSSEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGI 2329
Cdd:cd05169  161 WLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGDCFEVAMHREKFPEKVPFRLTRMLVNAMEVSGV 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 1019688  2330 EGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05169  241 EGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISW 277
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
1461-1845 2.00e-133

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


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 422.15  E-value: 2.00e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1461 APLAAGAAWGLGEWDMLEQYISVMKPKSPDKEFFDAILYLHKNDYDNASKHILNARDLLVTEISALINESYNRAYSVIVR 1540
Cdd:pfam02259    1 APLAAEAAWRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1541 TQIITEFEEIIKYKQLPPNSEKKL-HYQNLWTKRLLGCQKNVDLWQRVLRVRSLVIKPKQD-------LQIWIKFANLCR 1612
Cdd:pfam02259   81 LQQLAELEEIIQYKQKLGQSSEELkSLLQTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDvylggyhAEMWLKFANLAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1613 KSGRMRLANKALNMLLEGGNDPSLpntfkapPPVVYAQLKYIWATGAYKEALNHLIGFTSRLAHDLGLDPNNMIAQSvkl 1692
Cdd:pfam02259  161 KSGRFSLAEKALLKLLGEDPEEWL-------PEVVYAYAKYLWPTGEQQEALLKLREFLSCYLQKNGELLSGLEVIN--- 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1693 ssastAPYVEEYTKLLARCFLKQGEWRIATQPNWRNTNPDAILGSYLLATHFDKNWYKAWHNWALANFEVISMVQEETKL 1772
Cdd:pfam02259  231 -----PTNLEEFTELLARCYLLKGKWQAALGQNWAEEKSEEILQAYLLATQFDPSWYKAWHTWALFNFEVLRKEEQGKEE 305
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1019688    1773 NGgkndddddtavnndnvridgsilgsgsltingnrypLELIQRHVVPAIKGFFHSISLLETSCLQDTLRLLT 1845
Cdd:pfam02259  306 EG------------------------------------PEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2123-2366 1.46e-86

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: 283.04  E-value: 1.46e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2123 LKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSPKSGLLGWVPNSDTFHVLIREHRDAKKIPlnieh 2202
Cdd:smart00146    3 FKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKV----- 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2203 wvmlqMAPDYENLTLLQKIEVFTYALDNTKGQDLYKILWLKSRS-SETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNL 2281
Cdd:smart00146   78 -----LDLRSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDpSEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNI 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2282 MLDrITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGIEGSFRITCENVMRVLRDNKESLMAILEAFALD 2361
Cdd:smart00146  153 MLD-KTGHLFHIDFGFILGNGPKLFGFPERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYD 231

                    ....*
gi 1019688     2362 PLIHW 2366
Cdd:smart00146  232 GLPDW 236
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
229-279 6.30e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.96  E-value: 6.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1019688     229 KHAALLIITALAENCPYLLYQYLNSILDNIWRALRDPHLVIRIDASITLAK 279
Cdd:pfam13513    4 REAAALALGSLAEGGPDLLAPAVPELLPALLPLLNDDSDLVREAAAWALGR 54
 
Name Accession Description Interval E-value
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
279-2470 0e+00

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 1787.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   279 KCLSTLRNRDPQLTSQWVQRLATSCEYgFQVNTLECIHASLLVYKEILFlkdpFLNQVFDQMCLNCIAYENHKAKMIReK 358
Cdd:COG5032    1 DRLAQIIYALPSLLKDCFTEILLRKSD-VRSSLFDLLHVSFLDYKEKDE----RLSNVNDLVRNSTQSLLNTISNLIK-I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   359 IYQIVPLLASFNPQLFAgKYLHQIMDNYLEILTNAPANKIPHLkddkpqilisigdiayevGPDIAPYVKQILDYIeHDL 438
Cdd:COG5032   75 VKFVLPLKSFFLSPIFA-KLRALPMTKILCISADTYCLSLSIK------------------ALADDESLTTILKTI-REL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   439 QTKFKFRKKfenEIFYCIGRLAVPLGPVLGKLLnRNILDLMFKCPLSDYMQETFQILTERIPSLGPKINDELLNLVCSTL 518
Cdd:COG5032  135 LSKFLLRLR---LLFLFIGLLAQKFSEAQSKLF-FKLLLSILKEILSDAYEALLNDLLENLKSLKETLQNRLLPLLFNIS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   519 SGTPFIQPGSPMEIPSFSRErAREWRNKNILQKTGEsnddNNDIKIIIQAFRMLKNIKSRFSLVEFVRIVALSYIEHTDP 598
Cdd:COG5032  211 DGNYFKVEIGRKLLDHLNAL-GQILDCQKIAKITKS----FRSLPVIIKKFLNLLLIKVSYYLPSFFRLSLLSYLDHFET 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   599 RVRKLAALTSCEIYVKDNICKQTSLHSLNTVSEVLSKLLAITIADPLQDIRLEVLKNLNPCFDPQLAQPDNLRLLFTALH 678
Cdd:COG5032  286 DLFKTFLVTSCFLFFVDEICKPESEHLAEEVSEKLSKFLTIEIIDSFPEIRISALSSLLVIFDYHLALPDAVRLLFGESN 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   679 DESFNIQSVAMELVGRLSSVNPAYVIPSIRKILLELLTKLKFSTSSREKEETASLLCTLIRSSKDVAKPYIEPLLNVLLP 758
Cdd:COG5032  366 DKVFLISELALDSTGRLLRVLPARVLPSLFEFLLSLLTVLKISGLILEFEISAQLLCNLIRSSNQLLTSLISPYFLFILP 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   759 KFQDTSSTVASTALRTIGELSVVGGEDMKI-YLKDLFPLIIKTFQDQSNSFKREAALKALGQLAassGYVIDPLLDYPEL 837
Cdd:COG5032  446 KCIDSSNSEISYRVENLGELKDILGLDRITdYQALSLRLIIVSIQLRSFVFKREAINQIFKQLA---SIVIKPFLDYPKR 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   838 LGILVNILKTENSQNIRRQTVTLIGILGAIDPYRQKEREVTSTTDISTEQNAPPIdIALLMQGMSPSNDEYYTTVVIHCL 917
Cdd:COG5032  523 LDLPIKIVTVVYVALLRRPTEKLSGVLGSIDKYSHIESEEMSSSDFPWTKNPVGL-QLLAVYGFIRSIDDLYFTVSDPTL 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   918 LKILKDPSLSSYHTAVIQAIMHIFQTLGLKCVSFLDQIiPTILDVMRTCSQSLLEFYFQQ-LCSLIIIVRQHIRPHVDSI 996
Cdd:COG5032  602 IEILKLPVLSIVHSAIIEAIMLIKLSLGSESSQFEDLN-PSFLYIFSNNSISDILFYFQNfLELIVIAFFPLIRSEIIGI 680
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   997 FQAIKDFSSV-AKLQITLVSVIEAISKALEGEFKRLVPLTLTLFLVILE--NDKSSDKVLSRRVLRLLESFGPNLEGYSH 1073
Cdd:COG5032  681 VLISSLFSKTwILLKLLLIAFISKLISALQGELKMLAPTLFTLFLVLVEryLDVEYSSVSFKLLLVILVYFGGNLESLVL 760
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1074 LITPKIVQMAEFTSGNLQRSAIIT-IGKLAKDVDLFEMSSRIVHSLLRVLSSttSDELSKVIMNTLSLLLIQMGTSFAI- 1151
Cdd:COG5032  761 LILDLIVMLVEYTELGLQESIFIErLSQFFKFKNLSENASRLLPPLMDNLSK--SHELRCVSEDDVSALLIQLLTDRVIc 838
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1152 FIPVINEVLM-KKHIQHTIYDDLTNRILNNDVLPTKILEANTTDYKPAEQMEAADAGVAK-LPINQSVLKSAWNSSQQRT 1229
Cdd:COG5032  839 FIPVINSSLGdSRRIFLSLLAQLLDDSLKEESLPYNLNVDRGTDLREFFQTVKSKAEVLSmLPFVQSILFEAWNRVDFLL 918
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1230 KEDWQEWSKRLSIQLLKESPSHALRACSNLASMYYPLAKELFNTAFACVWTELYSQYQEDLIGSLCIALSSPLNPPEIHQ 1309
Cdd:COG5032  919 KDFWQEELDNLLVALLKELPFMALRDCSILSDLYFMLGRELWNSVSFECWLELMNSYKRLLIKSLKSKLHLPTIPILILQ 998
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1310 TLL---NLVEFMEHDDKALPIPTQSLGEYAERCHAYAKALHYKEIKFIKEPENSTIESLISINNQLNQTDAAIGILKHAQ 1386
Cdd:COG5032  999 MLLdskNLTEFTEHQLKNLPLPSLSIGFYESLCSFLAKLLHDEELYFFPLLFVSSLETLLSVNYHINQLDLRPNILKHFG 1078
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1387 QHHSLQLKETWFEKLERWEDALHAYNEREKAGDTSVSVTLGKMRSLHALGEWEQLSQLAARKWKVSKLQTKKLIAPLAAG 1466
Cdd:COG5032 1079 SFVRFQLKPHLVKYLQRWYEALNRYFELLSKGDRLFAISFTKLRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVAT 1158
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1467 AAWGLGEWDMLEQYISVMKPKSPDKEFFD--AILYLHKNDYDNASKHIL-NARDLLVTEISAL-INESYNRAYSVIVRTQ 1542
Cdd:COG5032 1159 AYEQVGEWYKAQQLYEVAQRKARSKEFPFslQYLYWHINDIDCADKLQSvLAELSLVTGISELlLEESWRRALFSNIKDS 1238
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1543 IITEFEEIIK--YKQLPPNSEK--KLHYQNLWTKRLLG---CQKNVDLWQRVLRVRSLVIKPKQDLQIWIKFANLCRKSG 1615
Cdd:COG5032 1239 LESELEEIIDgmYKSNEDFGALmlLSLSAELWDKILEGrssCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASS 1318
                       1370      1380      1390      1400      1410      1420      1430      1440
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1616 -RMRLANKALNMLLE-GGNDPSLPNTFKA--PPPVVYAQLKYIWATGAYKEALNHLIGFTSRLAHDLGLDPNNMIAQSVK 1691
Cdd:COG5032 1319 iRSKLLEKNIQELLEkLEEIKSPLGTLRDrlPPPWALLDLKRLLATWRQNAFLRINPELLPLLSSLLNLQSSSLSKQLVS 1398
                       1450      1460      1470      1480      1490      1500      1510      1520
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1692 LSSASTAPYVEEYTKLLARCFLKQGEWRIATQPNWRNTNPDAILGSYLLATHFDKNWYKAWHN-WALANFEVISMVQEET 1770
Cdd:COG5032 1399 RGSSESAISINSFASVARKHFLPDNQLKKIYQLSNILISEAFLLLRYLLLCRLGRRELKAGLNvWNLTNLELFSDIQESE 1478
                       1530      1540      1550      1560      1570      1580      1590      1600
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1771 KlnggkndddddtavnndnvridgsilgsgsltingNRYPLELIQRHVVPAIKGFFHSISLLETSCLQDTLRLLTLLFNF 1850
Cdd:COG5032 1479 F-----------------------------------FEWGKNLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELL 1523
                       1610      1620      1630      1640      1650      1660      1670      1680
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1851 GGIKEVSQAMYEGFNLMKIE-NWLEVLPQLISRIHQPDPTVSNSLLSLLSDLGKAHPQALVYPLTVAIKSESVSRQKAAL 1929
Cdd:COG5032 1524 GSLLSAKDAAGSYYKNFHIFdLEISVIPFIPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVAL 1603
                       1690      1700      1710      1720      1730      1740      1750      1760
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1930 SIIEKIRIHSPVLVNQAELVSHELIR-VAVLWHELWYEGLEDASRQFFVEHN-IEKMFSTLEPLHKHLGNEPQTLSEVSF 2007
Cdd:COG5032 1604 SLENKSRTHDPSLVKEALELSDENIRiAYPLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSF 1683
                       1770      1780      1790      1800      1810      1820      1830      1840
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2008 QKSFGRDLNDAYEWLNNYKKSKDINNLNQAWDIYYNVFRKITRQIPQLQTLDLQHVSPQLLATHD-LELAVPGTYFPGKP 2086
Cdd:COG5032 1684 QSSFLKELIKKSPRKIRKKFKIDISLLNLSRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAfLEIKLPGQYLLDKP 1763
                       1850      1860      1870      1880      1890      1900      1910      1920
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2087 TIRIAKFEPLFSVISS-KQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAI 2165
Cdd:COG5032 1764 FVLIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVI 1843
                       1930      1940      1950      1960      1970      1980      1990      2000
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2166 PLSPKSGLLGWVPNSDTFHVLIREHRDAKKIPLNIEHwvmlQMAPDYENLTLLQKIEVFTYALDNTKgQDLYKILWLKSR 2245
Cdd:COG5032 1844 PLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEK----KLAARLDNLKLLLKDEFFTKATLKSP-PVLYDWFSESFP 1918
                       2010      2020      2030      2040      2050      2060      2070      2080
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2246 SSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAME 2325
Cdd:COG5032 1919 NPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFGFILFNAPGRFPFPEKVPFRLTRNIVEAMG 1998
                       2090      2100      2110      2120      2130      2140      2150      2160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2326 VSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHWGFdlppqklteqtgipLPLInpsellrkgaitveeaanm 2405
Cdd:COG5032 1999 VSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR--------------LPCF------------------- 2045
                       2170      2180      2190      2200      2210      2220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1019688  2406 eaeqqNETKNARAMLVLRRITDKLTGNDIKRFNELDVPEQVDKLIQQATSIERLCQHYIGWCPFW 2470
Cdd:COG5032 2046 -----REIQNNEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
2090-2366 0e+00

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: 570.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05169    1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTFHVLIREHRDAKKIPLNIEHWVMLQMAPDYENLTLLQKIEVFTYALDNTKGQDLYKILWLKSRSSET 2249
Cdd:cd05169   81 NSGLIGWVPGCDTLHSLIRDYREKRKIPLNIEHRLMLQMAPDYDNLTLIQKVEVFEYALENTPGDDLRRVLWLKSPSSEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGI 2329
Cdd:cd05169  161 WLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGDCFEVAMHREKFPEKVPFRLTRMLVNAMEVSGV 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 1019688  2330 EGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05169  241 EGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISW 277
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
1461-1845 2.00e-133

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


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 422.15  E-value: 2.00e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1461 APLAAGAAWGLGEWDMLEQYISVMKPKSPDKEFFDAILYLHKNDYDNASKHILNARDLLVTEISALINESYNRAYSVIVR 1540
Cdd:pfam02259    1 APLAAEAAWRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1541 TQIITEFEEIIKYKQLPPNSEKKL-HYQNLWTKRLLGCQKNVDLWQRVLRVRSLVIKPKQD-------LQIWIKFANLCR 1612
Cdd:pfam02259   81 LQQLAELEEIIQYKQKLGQSSEELkSLLQTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDvylggyhAEMWLKFANLAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1613 KSGRMRLANKALNMLLEGGNDPSLpntfkapPPVVYAQLKYIWATGAYKEALNHLIGFTSRLAHDLGLDPNNMIAQSvkl 1692
Cdd:pfam02259  161 KSGRFSLAEKALLKLLGEDPEEWL-------PEVVYAYAKYLWPTGEQQEALLKLREFLSCYLQKNGELLSGLEVIN--- 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1693 ssastAPYVEEYTKLLARCFLKQGEWRIATQPNWRNTNPDAILGSYLLATHFDKNWYKAWHNWALANFEVISMVQEETKL 1772
Cdd:pfam02259  231 -----PTNLEEFTELLARCYLLKGKWQAALGQNWAEEKSEEILQAYLLATQFDPSWYKAWHTWALFNFEVLRKEEQGKEE 305
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1019688    1773 NGgkndddddtavnndnvridgsilgsgsltingnrypLELIQRHVVPAIKGFFHSISLLETSCLQDTLRLLT 1845
Cdd:pfam02259  306 EG------------------------------------PEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2118-2366 1.18e-90

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: 295.01  E-value: 1.18e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    2118 DYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRhldIQQYPAIPLSPKSGLLGWVPNSDTFHVLIREHRDaKKIP 2197
Cdd:pfam00454    1 GYGGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGE-NGVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    2198 LNIEHWvMLQMAPDYENLTLLqkievFTYALDNTKGQDLYKILWLKSRSSETWLERRTTYTRSLAVMSMTGYILGLGDRH 2277
Cdd:pfam00454   77 PTAMVK-ILHSALNYPKLKLE-----FESRISLPPKVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRH 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    2278 PSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGIEGSFRITCENVMRVLRDNKESLMAILEA 2357
Cdd:pfam00454  151 LDNILVDKTTGKLFHIDFGLCLPDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKL 230

                   ....*....
gi 1019688    2358 FALDPLIHW 2366
Cdd:pfam00454  231 MVADGLPDW 239
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
2090-2366 9.33e-88

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: 288.28  E-value: 9.33e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05171    1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRIRTYKVVPLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTFH-VLIREHRD----AKKIPLNIEHWVMLQMAPDYENLTLLQKIEVFTYALDNTKGQdLYKILWLKS 2244
Cdd:cd05171   81 RSGVLEFVENTIPLGeYLVGASSKsgahARYRPKDWTASTCRKKMREKAKASAEERLKVFDEICKNFKPV-FRHFFLEKF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2245 RSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAA-ILRekYPEKVPFRLTRMLTYA 2323
Cdd:cd05171  160 PDPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGkLLP--IPETVPFRLTRDIVDG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 1019688  2324 MEVSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05171  238 MGITGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSW 280
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2123-2366 1.46e-86

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: 283.04  E-value: 1.46e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2123 LKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSPKSGLLGWVPNSDTFHVLIREHRDAKKIPlnieh 2202
Cdd:smart00146    3 FKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKV----- 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2203 wvmlqMAPDYENLTLLQKIEVFTYALDNTKGQDLYKILWLKSRS-SETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNL 2281
Cdd:smart00146   78 -----LDLRSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDpSEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNI 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     2282 MLDrITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGIEGSFRITCENVMRVLRDNKESLMAILEAFALD 2361
Cdd:smart00146  153 MLD-KTGHLFHIDFGFILGNGPKLFGFPERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYD 231

                    ....*
gi 1019688     2362 PLIHW 2366
Cdd:smart00146  232 GLPDW 236
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
2090-2361 2.98e-84

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: 275.69  E-value: 2.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05164    1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTFHVLirehrdakkiplniehwvmlqmapdyenltllqkievftyaldntkgqdLYKILWLKSRSSET 2249
Cdd:cd05164   81 QSGLIEWVDNTTTLKPV-------------------------------------------------LKKWFNETFPDPTQ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKyPEKVPFRLTRMLTYAMEVSGI 2329
Cdd:cd05164  112 WYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFNKGKTLPV-PEIVPFRLTRNIINGMGPTGV 190
                        250       260       270
                 ....*....|....*....|....*....|..
gi 1019688  2330 EGSFRITCENVMRVLRDNKESLMAILEAFALD 2361
Cdd:cd05164  191 EGLFRKSCEQVLRVFRKHKDKLITFLDTFLYD 222
DUF3385 pfam11865
Domain of unknown function (DUF3385); This domain is functionally uncharacterized. This domain ...
827-986 1.23e-83

Domain of unknown function (DUF3385); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is typically between 160 to 172 amino acids in length. This domain is found associated with pfam00454, pfam02260, pfam02985, pfam02259 and pfam08771.


Pssm-ID: 463377  Cd Length: 160  Bit Score: 271.39  E-value: 1.23e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     827 VIDPLLDYPELLGILVNILKTENSQNIRRQTVTLIGILGAIDPYRQKEREVTSTTDISTEQNAPPIDIALLMQGMSPSND 906
Cdd:pfam11865    1 VIDPYLDYPQLLGILLNILKTEQSQSIRRETIRVLGILGALDPYKHKENEGKSEDSDSEEQNAPSTDVSLLMVGMSPSNE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688     907 EYYTTVVIHCLLKILKDPSLSSYHTAVIQAIMHIFQTLGLKCVSFLDQIIPTILDVMRTCSQSLLEFYFQQLCSLIIIVR 986
Cdd:pfam11865   81 EYYPTVVINSLMRILRDPSLSSHHTAVVQAIMFIFKTLGLKCVPFLPQVIPALLSVIRTCPPSLREFYFQQLATLVSIVK 160
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2090-2366 5.27e-81

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: 269.90  E-value: 5.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05170    1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPN------------------------------------SDTFHVLIREHRDAKKIPLNI--EHW---VMLQm 2208
Cdd:cd05170   81 RSGLIQWVDGatplfslykrwqqrraaaqaqknqdsgstpppvprpSELFYNKLKPALKAAGIRKSTsrREWpleVLRQ- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2209 apdyenltllqkieVFTYALDNTKGQDLYKILWLKSRSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITG 2288
Cdd:cd05170  160 --------------VLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTG 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1019688  2289 KVIHIDFGDCFEAAiLREKYPEKVPFRLTRMLTYAMEVSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05170  226 EVVHIDYNVCFEKG-KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDW 302
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
2090-2366 4.96e-80

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: 264.37  E-value: 4.96e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd00892    1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTF-HVLIREHRDakkiplnIEHWVMLQMAPDyenltllqkievftyaldntkgqdlykilwlksrsSE 2248
Cdd:cd00892   81 ECGIIEWVPNTVTLrSILSTLYPP-------VLHEWFLKNFPD-----------------------------------PT 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2249 TWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFgDC-FEAAiLREKYPEKVPFRLTRMLTYAMEVS 2327
Cdd:cd00892  119 AWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDF-DClFDKG-LTLEVPERVPFRLTQNMVDAMGVT 196
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 1019688  2328 GIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd00892  197 GVEGTFRRTCEVTLRVLRENRETLMSVLETFVHDPLVEW 235
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
2090-2366 1.64e-65

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: 222.45  E-value: 1.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIPLSP 2169
Cdd:cd05172    1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2170 KSGLLGWVPNSDTFHVLIRehRDAkkiplniehwvmLQMApdyenltlLQKIevftyaldntkgqdlykilwlkSRSSET 2249
Cdd:cd05172   81 RLGLIEWVDNTTPLKEILE--NDL------------LRRA--------LLSL----------------------ASSPEA 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYAMEVSGI 2329
Cdd:cd05172  117 FLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFGSATQFLPIPELVPFRLTRQLLNLLQPLDA 196
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 1019688  2330 EGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05172  197 RGLLRSDMVHVLRALRAGRDLLLATMDVFVKEPLLDW 233
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
2099-2361 3.60e-61

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: 209.11  E-value: 3.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2099 VISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkRHLDIQQYPAIPLSPKSGLLGWVP 2178
Cdd:cd00142   10 VIHSKQRPKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSILEKES----VNLVLPPYKVIPLSENSGLIEIVK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2179 NSDTFHvlirehrdakkiplniehwvmlqmapdyenltllqkievftyaldntkgqDLYKILWLKSRSSETWLERRTTYT 2258
Cdd:cd00142   86 DAQTIE--------------------------------------------------DLLKSLWRKSPSSQSWLNRRENFS 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2259 RSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGDCFEAAILREKyPEKVPFRLTRMLTYAMEVSGIEGSFRITCE 2338
Cdd:cd00142  116 CSLAGYSVLGYIFGIGDRHPSNIMIEP-SGNIFHIDFGFIFSGRKLAEG-VETVPFRLTPMLENAMGTAGVNGPFQISMV 193
                        250       260
                 ....*....|....*....|...
gi 1019688  2339 NVMRVLRDNKESLMAILEAFALD 2361
Cdd:cd00142  194 KIMEILREHADLIVPILEHSLRD 216
FRB_dom pfam08771
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ...
1952-2049 2.40e-55

FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.


Pssm-ID: 462596  Cd Length: 98  Bit Score: 187.79  E-value: 2.40e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688    1952 ELIRVAVLWHELWYEGLEDASRQFFVEHNIEKMFSTLEPLHKHLGNEPQTLSEVSFQKSFGRDLNDAYEWLNNYKKSKDI 2031
Cdd:pfam08771    1 ELIRVAILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDE 80
                           90
                   ....*....|....*...
gi 1019688    2032 NNLNQAWDIYYNVFRKIT 2049
Cdd:pfam08771   81 EDLNQAWDIYYSVFRRIK 98
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2082-2324 3.35e-23

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: 103.77  E-value: 3.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2082 FPGKPTIRIAKFEPL-FSVISSKQRPRKFSIKGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkrhLDIQ 2160
Cdd:cd00896   55 LPLDPSVKVTGIIPEkSTVFKSALMPLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKEN------LDLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2161 --QYPAIPLSPKSGLLGWVPNSDTFHVLIREHRdakkiplNIEHWVMlQMAPDYENLTLLQKievftyaldntkgqdlyk 2238
Cdd:cd00896  129 ltPYKVLATSPNDGLVEFVPNSKALADILKKYG-------SILNFLR-KHNPDESGPYGIKP------------------ 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2239 ilwlksrssetwlERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGdcFeaaIL-REKYPEKVPFRLT 2317
Cdd:cd00896  183 -------------EVMDNFVKSCAGYCVITYILGVGDRHLDNLLLTK-DGHLFHIDFG--Y---ILgRDPKPFPPPMKLC 243

                 ....*..
gi 1019688  2318 RMLTYAM 2324
Cdd:cd00896  244 KEMVEAM 250
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
2090-2366 9.60e-23

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: 99.90  E-value: 9.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2090 IAKFEPLFSVISSKQRP-RKFSIKGSDGKDYKYVLK--GHEDIRQDSLVMQLFGLVNTLLKNDSECFKRHLDIQQYPAIP 2166
Cdd:cd05163    1 IARFLPRVEIVRRHGTCyRRLTIRGHDGSKYPFLVQtpSARHSRREERVMQLFRLLNRVLERKKETRRRNLQFHVPIVVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2167 LSPKsgllgwvpnsdtfhvlIRehrdakkiplniehwvMLQMAPDYENL-TLLQKIEVFTYALDNTKGQDLYKILWLKS- 2244
Cdd:cd05163   81 LSPQ----------------VR----------------LVEDDPSYISLqDIYEKLEILNEIQSKMVPETILSNYFLRTm 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2245 -RSSETWLERRTtYTRSLAVMSMTGYILGLGDRHPSNLMLDRITGKVIHIDFGDCFEAAILREKYPEKVPFRLTRMLTYA 2323
Cdd:cd05163  129 pSPSDLWLFRKQ-FTLQLALSSFMTYVLSLGNRTPHRILISRSTGNVFMTDFLPSINSQGPLLDNNEPVPFRLTPNIQHF 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 1019688  2324 MEVSGIEGSFRITCENVMRVLRDNKESLMAILEAFALDPLIHW 2366
Cdd:cd05163  208 IGPIGVEGLLTSSMMAIARALTEPEYDLEQYLSLFVRDELISW 250
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2047-2347 2.59e-18

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: 88.78  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2047 KITRQIPQLQTLDLQHVSPQLLAthdlELAVPGTY-FPGKPTIRIAKFEPL-FSVISSKQRPRKFSIKGSD--GKDYKYV 2122
Cdd:cd00891   16 EIAKKIKEEPSEERKEVLEKLLQ----KLELPKKFtLPLDPRMEVKGLIVEkCKVMDSKKLPLWLVFKNADpgGDPIKVI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2123 LKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkrhLD--IQQYPAIPLSPKSGLLGWVPNSDTfhvLIREHRDAKKiplni 2200
Cdd:cd00891   92 FKAGDDLRQDQLTLQLLRIMDKLWKKEG------LDlrMTPYKCIATGDEVGMIEVVPNSET---TAAIQKKYGG----- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2201 ehwvmlqmapdyenltllqKIEVFTY-ALDNtkgqdlykilWLKSR-SSETWLER-RTTYTRSLAVMSMTGYILGLGDRH 2277
Cdd:cd00891  158 -------------------FGAAFKDtPISN----------WLKKHnPTEEEYEEaVENFIRSCAGYCVATYVLGIGDRH 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1019688  2278 PSNLMLDRiTGKVIHIDFG-----DCFEAAILRekypEKVPFRLTRMLTYAMevSGIEG----SFRITCENVMRVLRDN 2347
Cdd:cd00891  209 NDNIMVTK-SGHLFHIDFGhflgnFKKKFGIKR----ERAPFVFTPEMAYVM--GGEDSenfqKFEDLCCKAYNILRKH 280
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
2091-2363 8.75e-16

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


Pssm-ID: 270718 [Multi-domain]  Cd Length: 366  Bit Score: 81.63  E-value: 8.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2091 AKFEPLFSVISSKQrprkfsikgSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkRHLDIQQYPAIPLSPK 2170
Cdd:cd05174   79 SKMKPLWIMYSSEE---------AGAGNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEG----LDLRMTPYGCLSTGDK 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2171 SGLLGWVPNSDTF-HVLIREHRDAKKIPLNIEhwvmlqmapdyenltllqkievftyALDNtkgqdlykilWLKSRSSET 2249
Cdd:cd05174  146 TGLIEVVLHSDTIaNIQLNKSNMAATAAFNKD-------------------------ALLN----------WLKSKNPGD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTT-YTRSLAVMSMTGYILGLGDRHPSNLMLdRITGKVIHIDFGDCFeaAILREKY---PEKVPFRLTRMLTYAME 2325
Cdd:cd05174  191 ALDQAIEeFTLSCAGYCVATYVLGIGDRHSDNIMI-RESGQLFHIDFGHFL--GNFKTKFginRERVPFILTYDFVHVIQ 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 1019688  2326 VSGIEGS-----FRITCENVMRVLRDNKE---SLMAILEAFALDPL 2363
Cdd:cd05174  268 QGKTNNSekferFRGYCERAYTILRRHGLlflHLFALMKAAGLPEL 313
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
2439-2470 5.02e-15

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: 70.49  E-value: 5.02e-15
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1019688    2439 ELDVPEQVDKLIQQATSIERLCQHYIGWCPFW 2470
Cdd:pfam02260    1 PLSVEGQVDELIQEATDPENLAQMYIGWCPWW 32
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2099-2317 8.02e-15

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: 78.83  E-value: 8.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2099 VISSKQRPRKFSIKGSD-----GKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkrhLDIQQ--YPAIPLSPKS 2171
Cdd:cd05165   71 VMDSKKRPLWLVFENADplalsGEDIKIIFKNGDDLRQDMLTLQIIRIMDNIWKEEG------LDLRMlpYGCLSTGDNV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2172 GLLGWVPNSDTFhvlirehrdakkipLNIEhwvmlqmapdyenltlLQKIEVFTYALDntKGQdLYKilWLK--SRSSET 2249
Cdd:cd05165  145 GLIEVVRNAKTI--------------ANIQ----------------KKKGKVATLAFN--KDS-LHK--WLKekNKTGEK 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGDcfeaaIL---REKY---PEKVPFRLT 2317
Cdd:cd05165  190 YDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKE-NGQLFHIDFGH-----FLgnfKKKFgikRERVPFVLT 257
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2098-2317 2.05e-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: 74.25  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2098 SVISSKQRPRKFSIKGSD--GKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKndsecfKRHLDIQQ--YPAIPLSPKSGL 2173
Cdd:cd05166   68 SYFNSNALPLKLVFRNADprAEPISVIFKVGDDLRQDMLTLQLIRIMDKIWL------QEGLDLKMitFRCVPTGNKRGM 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2174 LGWVPNSDTfhvlirehrdakkiplniehwvmlqmapdyenltlLQKIEVFTYALDNTKGQDLYKILWLKSRSSETWLER 2253
Cdd:cd05166  142 VELVPEAET-----------------------------------LREIQTEHGLTGSFKDRPLADWLQKHNPSELEYEKA 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1019688  2254 RTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGDCFEAA-----ILRekypEKVPFRLT 2317
Cdd:cd05166  187 VENFIRSCAGYCVATYVLGICDRHNDNIMLKT-SGHLFHIDFGKFLGDAqmfgnFKR----DRVPFVLT 250
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2091-2347 1.09e-12

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: 72.30  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2091 AKFEPLFSVISSKqrprkfsikGSDGKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkRHLDIQQYPAIPLSPK 2170
Cdd:cd05173   76 SKMKPLWIVYNNK---------LFGGDSLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAG----LDLRIVPYGCLATGDR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2171 SGLLGWVPNSDTFhvlirehrdaKKIPLNIEHwvmLQMAPDYENLTLLQkievftyaldntkgqdlykilWLKSRSSETW 2250
Cdd:cd05173  143 SGLIEVVSSAETI----------ADIQLNSSN---VAAAAAFNKDALLN---------------------WLKEYNSGDD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2251 LERRTT-YTRSLAVMSMTGYILGLGDRHPSNLMLdRITGKVIHIDFGDCFeaAILREKYP---EKVPFRLTRMLTYAME- 2325
Cdd:cd05173  189 LERAIEeFTLSCAGYCVATYVLGIGDRHSDNIMV-RKNGQLFHIDFGHIL--GNFKSKFGikrERVPFILTYDFIHVIQq 265
                        250       260
                 ....*....|....*....|....*.
gi 1019688  2326 --VSGIE--GSFRITCENVMRVLRDN 2347
Cdd:cd05173  266 gkTGNTEkfGRFRQYCEDAYLILRKN 291
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
2097-2338 3.91e-12

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: 69.54  E-value: 3.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2097 FSVISSKQRPRKFSIKGSDGKD---YKYVLKGHEDIRQDSLVMQLFGLvntlLKNdseCFKRH-LDIQQYP--AIPLSPK 2170
Cdd:cd05167   25 FKVKDCGVDELEHEGTESEATKevwQAAIFKVGDDCRQDMLALQLISL----FKN---IFEEVgLDLYLFPyrVVATGPG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2171 SGLLGWVPNSDTfhvlirehRDakkiplniehwvmlQMAPDYENltllqkievftyaldntkgqDLYKILWLK--SRSSE 2248
Cdd:cd05167   98 CGVIEVIPNSKS--------RD--------------QIGRETDN--------------------GLYEYFLSKygDESTP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2249 TWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGDCFEAAilrekyP------EKVPFRLTRMLTY 2322
Cdd:cd05167  136 AFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDD-DGHIIHIDFGFIFEIS------PggnlgfESAPFKLTKEMVD 208
                        250
                 ....*....|....*.
gi 1019688  2323 AMEVSGIEGSFRITCE 2338
Cdd:cd05167  209 LMGGSMESEPFKWFVE 224
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
2122-2358 1.40e-10

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: 64.59  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2122 VLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkRHLDIQQYPAIPLSPKSGLLGWVPNSDTFHVLIREhrdakkiplnie 2201
Cdd:cd00893   31 IVKTGDDLKQEQLALQLISQFDQIFKEEG----LPLWLRPYEILSLGPDSGIIEMIKNAVSIDSLKKK------------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2202 hwvmlqmapdyenltlLQKIevftyaldnTKGQDLYKILwLKSRSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNL 2281
Cdd:cd00893   95 ----------------LDSF---------NKFVSLSDFF-DDNFGDEAIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2282 MLDRiTGKVIHIDFGDCFEAAilrekyP-----EKVPFRLTRmlTYAMEVSGIEGS----FRITCENVMRVLRDNKESLM 2352
Cdd:cd00893  149 LLDK-EGHIIHIDFGFFLSSH------PgfygfEGAPFKLSS--EYIEVLGGVDSElfkeFRKLFLKGFMALRKHSDKIL 219

                 ....*.
gi 1019688  2353 AILEAF 2358
Cdd:cd00893  220 SLVEMM 225
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
2124-2356 2.45e-09

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: 60.96  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2124 KGHEDIRQDSLVMQLFglvnTLLKNdseCFKRH---LDIQQYPAIPLSPKSGLLGWVPNSDTFHVLirehrdaKKiplni 2200
Cdd:cd05168   36 KSGDDLRQELLAMQLI----KQFQR---IFEEAglpLWLRPYEILVTSSDSGLIETIPDTVSIDSL-------KK----- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2201 ehwvmlqMAPDYENLTllqkiEVFTYALDNtkgqdlykilwlksRSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSN 2280
Cdd:cd05168   97 -------RFPNFTSLL-----DYFERTFGD--------------PNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2281 LMLDRiTGKVIHIDFGDC---------FEAAilrekypekvPFRLTRMLtyaMEVSGIEGS-----FRITCENVMRVLRD 2346
Cdd:cd05168  151 ILLDS-EGHIIHIDFGFMlsnspgglgFETA----------PFKLTQEY---VEVMGGLESdmfryFKTLMIQGFLALRK 216
                        250
                 ....*....|
gi 1019688  2347 NKESLMAILE 2356
Cdd:cd05168  217 HADRIVLLVE 226
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
2098-2324 5.54e-08

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


Pssm-ID: 270720 [Multi-domain]  Cd Length: 353  Bit Score: 57.30  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2098 SVISSKQRPRKFSIKGSD--GKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLkndsecFKRHLDIQQ--YPAIPLSPKSGL 2173
Cdd:cd05176   68 SFFSSNAVPLKVALVNADplGEEINVMFKVGEDLRQDMLALQMIKIMDKIW------LQEGLDLRMviFKCLSTGKDRGM 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2174 LGWVPNSDTfhvlirehrdakkiplniehwvmlqmapdyenltlLQKIEVFTYALDNTKGQDLYKILWLKSRSSETWLER 2253
Cdd:cd05176  142 VELVPSSDT-----------------------------------LRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKA 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1019688  2254 RTTYTRSLAVMSMTGYILGLGDRHPSNLMLdRITGKVIHIDFGDCFEAAILREKYP-EKVPFRLTRMLTYAM 2324
Cdd:cd05176  187 SENFIYSCAGCCVATYVLGICDRHNDNIML-RSTGHMFHIDFGKFLGHAQMFGSFKrDRAPFVLTSDMAYVI 257
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
2099-2318 3.55e-07

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: 55.06  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2099 VISSKQRPRKFSIKGSD------GKDYKYVLKGHEDIRQDSLVMQLFGLVNTLLKNDSecfkrhLDIQQYP--AIPLSPK 2170
Cdd:cd05175   77 IMSSAKRPLWLNWENPDimsellFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQG------LDLRMLPygCLSIGDC 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2171 SGLLGWVPNSDTFhvlirehrdakkipLNIEHWVMLQMAPDYENLTLLQkievftyaldntkgqdlykilWLKSRSS-ET 2249
Cdd:cd05175  151 VGLIEVVRNSHTI--------------MQIQCKGGLKGALQFNSHTLHQ---------------------WLKDKNKgEI 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2250 WLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLdRITGKVIHIDFGDCFEAAILREKYP-EKVPFRLTR 2318
Cdd:cd05175  196 YDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMV-KDDGQLFHIDFGHFLDHKKKKFGYKrERVPFVLTQ 264
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2241-2360 1.71e-05

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: 49.48  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2241 WLKSRS--SETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFGDC---FEAAILREKypEKVPFR 2315
Cdd:cd00894  182 WLKEKCpiEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITE-TGNLFHIDFGHIlgnYKSFLGINK--ERVPFV 258
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 1019688  2316 LTRMLTYAMEVSGIEGS-----FRITCENVMRVLRdNKESLMAILEAFAL 2360
Cdd:cd00894  259 LTPDFLFVMGTSGKKTSlhfqkFQDVCVKAYLALR-HHTNLLIILFSMML 307
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2098-2324 7.66e-05

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


Pssm-ID: 119421 [Multi-domain]  Cd Length: 354  Bit Score: 47.69  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2098 SVISSKQRPRKFSIKGSD--GKDYKYVLKGHEDIRQDSLVMQLFGLVNTLlkndsecfkrhldiqqypaiplspksgllg 2175
Cdd:cd00895   69 SYFNSNAVPLKLSFQNVDplGENIRVIFKCGDDLRQDMLTLQMIRIMNKI------------------------------ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2176 WVPNS-DTFHVLIREHRDAKKIPlniehwvMLQMAPDYENLtllQKIEVFTYALDNTKGQDLYKILWLKSRSSETWLERR 2254
Cdd:cd00895  119 WVQEGlDMRMVIFRCFSTGRGRG-------MVEMIPNAETL---RKIQVEHGVTGSFKDRPLADWLQKHNPTEDEYEKAV 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1019688  2255 TTYTRSLAVMSMTGYILGLGDRHPSNLMLdRITGKVIHIDFGDCF-EAAILREKYPEKVPFRLTRMLTYAM 2324
Cdd:cd00895  189 ENFIYSCAGCCVATYVLGICDRHNDNIML-KTTGHMFHIDFGRFLgHAQMFGNIKRDRAPFVFTSDMAYVI 258
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2082-2296 5.51e-04

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: 44.88  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2082 FPGKPTIRIAKFEP-LFSVISSKQRPRKFSIKGSD--GKDYKYVLKGHEDIRQDSLVMQLFGLVntllknDSECFKRHLD 2158
Cdd:cd05177   52 LPLNPALRVKGIDAdACSYFTSNAAPLKISFINANplAKNISIIFKTGDDLRQDMLVLQIVRVM------DNIWLQEGLD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2159 IQQ--YPAIPLSPKSGLLGWVPNSDTfhvLIREHRdakkiplnieHWVMLqmAPDYENltllqkievftyaldntkgqDL 2236
Cdd:cd05177  126 MQMiiYRCLSTGKTQGLVQMVPDAVT---LAKIHR----------ESGLI--GPLKEN--------------------TI 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  2237 YKILWLKSRSSETWLERRTTYTRSLAVMSMTGYILGLGDRHPSNLMLDRiTGKVIHIDFG 2296
Cdd:cd05177  171 EKWFHMHNKLKEDYDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTH-SGHMFHIDFG 229
KAP95 COG5215
Karyopherin (importin) beta [Intracellular trafficking and secretion];
675-849 1.49e-03

Karyopherin (importin) beta [Intracellular trafficking and secretion];


Pssm-ID: 227540 [Multi-domain]  Cd Length: 858  Bit Score: 44.16  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   675 TALHDESFNIQSVAMELVGRLSSVNPAYVIPSIRKILLELLTKLKFSTSSREK----------EETASLLCTL----IRS 740
Cdd:COG5215  507 TELALNESNLRVSLFSALGTLILICPDAVSDILAGFYDYTSKKLDECISVLGQilatedqllvEELQSNYIGVleaiIRT 586
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   741 SKDVAKPYIEPLLNVLLPKFQDTSSTVA-STALRTIGELSVVGGEDMKIYLKDLFPLIIKTFqDQSNSFKREAALKALGQ 819
Cdd:COG5215  587 RRRDIEDVEDQLMELFIRILESTKPTTAfGDVYTAISALSTSLEERFEQYASKFIPYLTRAL-NCTDRFVLNSAVGLVGD 665
                        170       180       190
                 ....*....|....*....|....*....|
gi 1019688   820 LAASSGYVIDPLLDypELLGILVNILKTEN 849
Cdd:COG5215  666 LANTLGTDFNIYAD--VLMSSLVQCLSSEA 693
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
771-820 2.89e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 38.12  E-value: 2.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1019688     771 ALRTIGELSVVGGEDMKIYLKDLFPLIIKTFQDqSNSFKREAALKALGQL 820
Cdd:pfam13513    7 AALALGSLAEGGPDLLAPAVPELLPALLPLLND-DSDLVREAAAWALGRL 55
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
810-864 3.45e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 37.73  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1019688     810 REAALKALGQLAASSGYVIDPLLdyPELLGILVNILKTENsQNIRRQTVTLIGIL 864
Cdd:pfam13513    4 REAAALALGSLAEGGPDLLAPAV--PELLPALLPLLNDDS-DLVREAAAWALGRL 55
HEAT COG1413
HEAT repeat [General function prediction only];
663-821 4.03e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 40.00  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   663 QLAQPDNLRLLFTALHDESFNIQSVAMELVGRLSSvnpayviPSIRKILLELLtklkfstssreKEETASLLCTLIRSSK 742
Cdd:COG1413   11 RLGDPAAVPALIAALADEDPDVRAAAARALGRLGD-------PRAVPALLEAL-----------KDPDPEVRAAAAEALG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   743 DVAKP-YIEPLLNVLlpkfQDTSSTVASTALRTIGELSVvggedmkiylKDLFPLIIKTFQDQsNSFKREAALKALGQLA 821
Cdd:COG1413   73 RIGDPeAVPALIAAL----KDEDPEVRRAAAEALGRLGD----------PAAVPALLEALKDP-DWEVRRAAARALGRLG 137
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
229-279 6.30e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.96  E-value: 6.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1019688     229 KHAALLIITALAENCPYLLYQYLNSILDNIWRALRDPHLVIRIDASITLAK 279
Cdd:pfam13513    4 REAAALALGSLAEGGPDLLAPAVPELLPALLPLLNDDSDLVREAAAWALGR 54
KAP95 COG5215
Karyopherin (importin) beta [Intracellular trafficking and secretion];
993-1161 9.42e-03

Karyopherin (importin) beta [Intracellular trafficking and secretion];


Pssm-ID: 227540 [Multi-domain]  Cd Length: 858  Bit Score: 41.46  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688   993 VDSIFQAIKDFSSVAKLQITLVSVIEAISKALEGEFKRLVPLTLTLFLVILENDKSS---DKVLSrRVLRLLESFGPNLE 1069
Cdd:COG5215  556 VLGQILATEDQLLVEELQSNYIGVLEAIIRTRRRDIEDVEDQLMELFIRILESTKPTtafGDVYT-AISALSTSLEERFE 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019688  1070 GYSHLITPKIVQMAEFTSGNLQRSAIITIGKLAK--DVDLFEMSSRIVHSLLRVLSSTTSD-ELSKVIMNTLSLLLIQMG 1146
Cdd:COG5215  635 QYASKFIPYLTRALNCTDRFVLNSAVGLVGDLANtlGTDFNIYADVLMSSLVQCLSSEATHrDLKPAILSVFGDIALAIG 714
                        170
                 ....*....|....*
gi 1019688  1147 tsfAIFIPVINEVLM 1161
Cdd:COG5215  715 ---ANFESYLDMIMM 726
 
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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