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Conserved domains on  [gi|189339266|ref|NP_063917|]
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serine/threonine-protein kinase ATR [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 2290-2564 2.15e-153

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: 474.69  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKIYkekgvymtgkelrqcmlpksaalseklkvfqelllprhPPVFHEWFLRTFPDPTSWYS 2449
Cdd:cd00892    81 ECGIIEWVPNTVTLRSILSTLY--------------------------------------PPVLHEWFLKNFPDPTAWYE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2450 SRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLF 2529
Cdd:cd00892   123 ARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTF 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 189339266 2530 RRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSK 2564
Cdd:cd00892   203 RRTCEVTLRVLRENRETLMSVLETFVHDPLVEWSR 237
TEL1 super family cl34875
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2123-2641 5.98e-91

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


The actual alignment was detected with superfamily member COG5032:

Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 331.75  E-value: 5.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2123 NSVLTEHTNRLAP---YQFLTAFSQLISRICHSHDEvfvvlmeIIAKVFLAYPQQAMWMMTAVSKSSYPMRVNRCKEILT 2199
Cdd:COG5032  1621 LELSDENIRIAYPllhLLFEPILAQLLSRLSSENNK-------ISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIK 1693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2200 KAihMKKSLEKFVGDATRLtDKLLELCNKSV----DGSNSTLSMSTHFKMLKRLvEDPTFSEILIPLQSVMIPTLPsvlg 2275
Cdd:COG5032  1694 KS--PRKIRKKFKIDISLL-NLSRKLYISVLrsirKRLKRLLELRLKKVSPKLL-LFHAFLEIKLPGQYLLDKPFV---- 1765

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2276 ahanhdpfpghwaYLAGFDDVVEILSS-LQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRR 2354
Cdd:COG5032  1766 -------------LIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRR 1832

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2355 RELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYMTGKELRQCMLpKSAALSEKLKVFqELLLPRHPPVFH 2434
Cdd:COG5032  1833 RDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKKLAARL-DNLKLLLKDEFF-TKATLKSPPVLY 1910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2435 EWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDF-NCLFNKGETFEVPEIVPFRLT 2513
Cdd:COG5032  1911 DWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFgFILFNAPGRFPFPEKVPFRLT 1990

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2514 HNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSKpVKGHSKAPLNETgevvnekakTHVLDIE 2593
Cdd:COG5032  1991 RNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR-LPCFREIQNNEI---------VNVLERF 2060

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 189339266 2594 QR-LQGviktRNRVTGLPLSIEGHVHYLIQEATDENLLCQMYLGWTPYM 2641
Cdd:COG5032  2061 RLkLSE----KDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1771-2092 9.21e-56

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


:

Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 198.73  E-value: 9.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1771 NTYRVEAAWKLSQWDLVENYLAADgKSTTWSVRLGQLLLSAKKRDTTTFYDTLKLVRAEQIVPLSAASFErgSYQRGYEF 1850
Cdd:pfam02259    1 APLAAEAAWRLGQWDLMREYLSLM-KKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGE--SYNRAYPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1851 IVRLHMLCELEHSLKPLFRKSPGDSCNEDSL-NWGARLEMTQNSYRAKEPILALRRALLSLNKRPDYNEMVGECWLQSAR 1929
Cdd:pfam02259   78 LVRLQQLAELEEIIQYKQKLGQSSEELKSLLqTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDVYLGGYHAEMWLKFAN 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1930 VARKAGHHQTAYNALLNAGESR----LAELYVERAKWLWSKGDVHQALIVLQKGVELCFPENKSPS-----------ESK 1994
Cdd:pfam02259  158 LARKSGRFSLAEKALLKLLGEDpeewLPEVVYAYAKYLWPTGEQQEALLKLREFLSCYLQKNGELLsglevinptnlEEF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1995 HMLIhGRATLLVGRFMEET----ANFESNAVMKKYKDVTLFLPEWEDGHFYLAKYYDKLMPMVTDNKMEK-QGDLIRYIV 2069
Cdd:pfam02259  238 TELL-ARCYLLKGKWQAALgqnwAEEKSEEILQAYLLATQFDPSWYKAWHTWALFNFEVLRKEEQGKEEEgPEDLSRYVV 316

                          330       340
                   ....*....|....*....|....*.
gi 189339266  2070 L---HFGRSLQYGNQFIYQSMPRMLS 2092
Cdd:pfam02259  317 PaveGYLRSLSLSSENSLQDTLRLLT 342
UME smart00802
Domain in UVSB PI-3 kinase, MEI-41 and ESR-1; Characteristic domain in UVSP PI-3 kinase, ...
 1119-1225 1.02e-31

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


:

Pssm-ID: 214825  Cd Length: 107  Bit Score: 120.77  E-value: 1.02e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   1119 MADYLQPKLLGILAFFNMQLLSSS--VGIEDKKMALTSLMSLMKLMGpKHVSSVRVKMMTTLRTGLRfKDDFPELCCRAW 1196
Cdd:smart00802    1 LADFLKDHFLGILAVFSNILHDSSgkKPYNEKKRALRSIGFLIKLMG-KHISSALPQIMACLQSALE-IPELRSLALRCW 78

                            90       100
                    ....*....|....*....|....*....
gi 189339266   1197 DCFVRCLDHAYLGPLLSHVIVALLPLIHM 1225
Cdd:smart00802   79 HVLIKTLKEEELGPLLDQIFAAILPLWPT 107
NR_LBD super family cl11397
The ligand binding domain of nuclear receptors, a family of ligand-activated transcription ...
 1529-1607 1.86e-03

The ligand binding domain of nuclear receptors, a family of ligand-activated transcription regulators; Ligand-binding domain (LBD) of nuclear receptor (NR): Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions in metazoans, from development, reproduction, to homeostasis and metabolism. The superfamily contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. The members of the family include receptors of steroids, thyroid hormone, retinoids, cholesterol by-products, lipids and heme. With few exceptions, NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD).


The actual alignment was detected with superfamily member cd07069:

Pssm-ID: 472173 [Multi-domain]  Cd Length: 241  Bit Score: 42.71  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 1529 LPHILVYvLLGCnQEDQQEVYAEIMAVLKHdEQHAISTQDSASD---LCQLSTQTVFSVLdhltQWARHK--FQALNAE- 1602
Cdd:cd07069     1 IPHLILE-LLKC-EPDEPQVQAKIMAYLQQ-EQANRSKHEKLSTfglMCKMADQTLFSIV----EWARSSifFRELKVDd 73


                  ....*..
gi 189339266 1603 --KLAQN 1607
Cdd:cd07069    74 qmKLLQN 80
 
Name Accession Description Interval E-value
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 2290-2564 2.15e-153

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: 474.69  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKIYkekgvymtgkelrqcmlpksaalseklkvfqelllprhPPVFHEWFLRTFPDPTSWYS 2449
Cdd:cd00892    81 ECGIIEWVPNTVTLRSILSTLY--------------------------------------PPVLHEWFLKNFPDPTAWYE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2450 SRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLF 2529
Cdd:cd00892   123 ARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTF 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 189339266 2530 RRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSK 2564
Cdd:cd00892   203 RRTCEVTLRVLRENRETLMSVLETFVHDPLVEWSR 237
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 2321-2564 1.21e-91

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: 297.67  E-value: 1.21e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2321 MMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYMTG 2400
Cdd:smart00146    1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2401 kelrqcmLPKSAALSEKLKVFQELLLPRHPPVFHEWFLRTFPDP-TSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENIL 2479
Cdd:smart00146   81 -------RSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIM 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2480 FDSfTGECVHVDFNCLFNKGETFEVP-EIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDP 2558
Cdd:smart00146  154 LDK-TGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDG 232


                    ....*.
gi 189339266   2559 LVEWSK 2564
Cdd:smart00146  233 LPDWRS 238
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2123-2641 5.98e-91

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 331.75  E-value: 5.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2123 NSVLTEHTNRLAP---YQFLTAFSQLISRICHSHDEvfvvlmeIIAKVFLAYPQQAMWMMTAVSKSSYPMRVNRCKEILT 2199
Cdd:COG5032  1621 LELSDENIRIAYPllhLLFEPILAQLLSRLSSENNK-------ISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIK 1693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2200 KAihMKKSLEKFVGDATRLtDKLLELCNKSV----DGSNSTLSMSTHFKMLKRLvEDPTFSEILIPLQSVMIPTLPsvlg 2275
Cdd:COG5032  1694 KS--PRKIRKKFKIDISLL-NLSRKLYISVLrsirKRLKRLLELRLKKVSPKLL-LFHAFLEIKLPGQYLLDKPFV---- 1765

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2276 ahanhdpfpghwaYLAGFDDVVEILSS-LQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRR 2354
Cdd:COG5032  1766 -------------LIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRR 1832

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2355 RELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYMTGKELRQCMLpKSAALSEKLKVFqELLLPRHPPVFH 2434
Cdd:COG5032  1833 RDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKKLAARL-DNLKLLLKDEFF-TKATLKSPPVLY 1910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2435 EWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDF-NCLFNKGETFEVPEIVPFRLT 2513
Cdd:COG5032  1911 DWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFgFILFNAPGRFPFPEKVPFRLT 1990

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2514 HNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSKpVKGHSKAPLNETgevvnekakTHVLDIE 2593
Cdd:COG5032  1991 RNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR-LPCFREIQNNEI---------VNVLERF 2060

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 189339266 2594 QR-LQGviktRNRVTGLPLSIEGHVHYLIQEATDENLLCQMYLGWTPYM 2641
Cdd:COG5032  2061 RLkLSE----KDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 2322-2563 4.30e-70

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 236.07  E-value: 4.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2322 MCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRelhIRTYAVIPLNDECGIIEWVNNTAGLRPILTKiYKEKGVYMTGk 2401
Cdd:pfam00454    5 IYKVGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDE-YGENGVPPTA- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2402 eLRQCMLPKSAALSEKLKVFQELLLPRhPPVFHEWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFD 2481
Cdd:pfam00454   80 -MVKILHSALNYPKLKLEFESRISLPP-KVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2482 SFTGECVHVDFN-CLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLV 2560
Cdd:pfam00454  158 KTTGKLFHIDFGlCLPDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLP 237


                   ...
gi 189339266  2561 EWS 2563
Cdd:pfam00454  238 DWS 240
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1771-2092 9.21e-56

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


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 198.73  E-value: 9.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1771 NTYRVEAAWKLSQWDLVENYLAADgKSTTWSVRLGQLLLSAKKRDTTTFYDTLKLVRAEQIVPLSAASFErgSYQRGYEF 1850
Cdd:pfam02259    1 APLAAEAAWRLGQWDLMREYLSLM-KKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGE--SYNRAYPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1851 IVRLHMLCELEHSLKPLFRKSPGDSCNEDSL-NWGARLEMTQNSYRAKEPILALRRALLSLNKRPDYNEMVGECWLQSAR 1929
Cdd:pfam02259   78 LVRLQQLAELEEIIQYKQKLGQSSEELKSLLqTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDVYLGGYHAEMWLKFAN 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1930 VARKAGHHQTAYNALLNAGESR----LAELYVERAKWLWSKGDVHQALIVLQKGVELCFPENKSPS-----------ESK 1994
Cdd:pfam02259  158 LARKSGRFSLAEKALLKLLGEDpeewLPEVVYAYAKYLWPTGEQQEALLKLREFLSCYLQKNGELLsglevinptnlEEF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1995 HMLIhGRATLLVGRFMEET----ANFESNAVMKKYKDVTLFLPEWEDGHFYLAKYYDKLMPMVTDNKMEK-QGDLIRYIV 2069
Cdd:pfam02259  238 TELL-ARCYLLKGKWQAALgqnwAEEKSEEILQAYLLATQFDPSWYKAWHTWALFNFEVLRKEEQGKEEEgPEDLSRYVV 316

                          330       340
                   ....*....|....*....|....*.
gi 189339266  2070 L---HFGRSLQYGNQFIYQSMPRMLS 2092
Cdd:pfam02259  317 PaveGYLRSLSLSSENSLQDTLRLLT 342
UME smart00802
Domain in UVSB PI-3 kinase, MEI-41 and ESR-1; Characteristic domain in UVSP PI-3 kinase, ...
 1119-1225 1.02e-31

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


Pssm-ID: 214825  Cd Length: 107  Bit Score: 120.77  E-value: 1.02e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   1119 MADYLQPKLLGILAFFNMQLLSSS--VGIEDKKMALTSLMSLMKLMGpKHVSSVRVKMMTTLRTGLRfKDDFPELCCRAW 1196
Cdd:smart00802    1 LADFLKDHFLGILAVFSNILHDSSgkKPYNEKKRALRSIGFLIKLMG-KHISSALPQIMACLQSALE-IPELRSLALRCW 78

                            90       100
                    ....*....|....*....|....*....
gi 189339266   1197 DCFVRCLDHAYLGPLLSHVIVALLPLIHM 1225
Cdd:smart00802   79 HVLIKTLKEEELGPLLDQIFAAILPLWPT 107
UME pfam08064
UME (NUC010) domain; This domain is characteriztic of UVSB PI-3 kinase, MEI-41 and ESR1.
 1122-1223 4.74e-27

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


Pssm-ID: 462350  Cd Length: 102  Bit Score: 107.19  E-value: 4.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1122 YLQPKLLGILAFFNMQLLSSSV--GIEDKKMALTSLMSLMKLMGPkHVSSVRVKMMTTLRTGLRfKDDFPELCCRAWDCF 1199
Cdd:pfam08064    1 FLENHILGILARFSDVLNDLRGkkPVEEKKRALRSIEELIKLMGS-AISSALPQIMACLQSALE-IPELREVALSCWDAF 78

                           90       100
                   ....*....|....*....|....
gi 189339266  1200 VRCLDHAYLGPLLSHVIVALLPLI 1223
Cdd:pfam08064   79 VKTLDEEDLGPLLDQTFAAILQLW 102
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
 2610-2641 3.29e-12

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


Pssm-ID: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 62.78  E-value: 3.29e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 189339266  2610 PLSIEGHVHYLIQEATDENLLCQMYLGWTPYM 2641
Cdd:pfam02260    1 PLSVEGQVDELIQEATDPENLAQMYIGWCPWW 32
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 1529-1607 1.86e-03

The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor superfamily,; The ligand binding domain (LBD) of the liver receptor homolog-1 (LRH-1): LRH-1 belongs to nuclear hormone receptor superfamily, and is expressed mainly in the liver, intestine, exocrine pancreas, and ovary. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 binds DNA as a monomer, and is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. Recently, phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, LRH-1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132754 [Multi-domain]  Cd Length: 241  Bit Score: 42.71  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 1529 LPHILVYvLLGCnQEDQQEVYAEIMAVLKHdEQHAISTQDSASD---LCQLSTQTVFSVLdhltQWARHK--FQALNAE- 1602
Cdd:cd07069     1 IPHLILE-LLKC-EPDEPQVQAKIMAYLQQ-EQANRSKHEKLSTfglMCKMADQTLFSIV----EWARSSifFRELKVDd 73


                  ....*..
gi 189339266 1603 --KLAQN 1607
Cdd:cd07069    74 qmKLLQN 80
 
Name Accession Description Interval E-value
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 2290-2564 2.15e-153

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: 474.69  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKIYkekgvymtgkelrqcmlpksaalseklkvfqelllprhPPVFHEWFLRTFPDPTSWYS 2449
Cdd:cd00892    81 ECGIIEWVPNTVTLRSILSTLY--------------------------------------PPVLHEWFLKNFPDPTAWYE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2450 SRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLF 2529
Cdd:cd00892   123 ARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTF 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 189339266 2530 RRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSK 2564
Cdd:cd00892   203 RRTCEVTLRVLRENRETLMSVLETFVHDPLVEWSR 237
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 2291-2557 3.67e-112

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: 355.81  E-value: 3.67e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2291 AGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLNDE 2370
Cdd:cd05164     2 ASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSSQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2371 CGIIEWVNNTAGLRPiltkiykekgvymtgkelrqcmlpksaalseklkvfqelllprhppVFHEWFLRTFPDPTSWYSS 2450
Cdd:cd05164    82 SGLIEWVDNTTTLKP----------------------------------------------VLKKWFNETFPDPTQWYEA 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2451 RSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFR 2530
Cdd:cd05164   116 RSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIINGMGPTGVEGLFR 195

                         250       260
                  ....*....|....*....|....*..
gi 189339266 2531 RACEVTLRLMRDQREPLMSVLKTFLHD 2557
Cdd:cd05164   196 KSCEQVLRVFRKHKDKLITFLDTFLYD 222
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 2291-2563 2.45e-100

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: 324.49  E-value: 2.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2291 AGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCrLME--FnSLINKSLRKDAESRRRELHIRTYAVIPLN 2368
Cdd:cd05171     2 SRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDA-VMEqvF-ELVNQLLKRDKETRKRKLRIRTYKVVPLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2369 DECGIIEWVNNTAGLRPILTKIYKEKGV-------YMTGKELRQCMLPKS-AALSEKLKVFQELLLpRHPPVFHEWFLRT 2440
Cdd:cd05171    80 PRSGVLEFVENTIPLGEYLVGASSKSGAharyrpkDWTASTCRKKMREKAkASAEERLKVFDEICK-NFKPVFRHFFLEK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2441 FPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGM 2520
Cdd:cd05171   159 FPDPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGKLLPIPETVPFRLTRDIVDGM 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 189339266 2521 GPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWS 2563
Cdd:cd05171   239 GITGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSWT 281
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 2321-2564 1.21e-91

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: 297.67  E-value: 1.21e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2321 MMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYMTG 2400
Cdd:smart00146    1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2401 kelrqcmLPKSAALSEKLKVFQELLLPRHPPVFHEWFLRTFPDP-TSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENIL 2479
Cdd:smart00146   81 -------RSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDPsEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIM 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   2480 FDSfTGECVHVDFNCLFNKGETFEVP-EIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDP 2558
Cdd:smart00146  154 LDK-TGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDG 232


                    ....*.
gi 189339266   2559 LVEWSK 2564
Cdd:smart00146  233 LPDWRS 238
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2123-2641 5.98e-91

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 331.75  E-value: 5.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2123 NSVLTEHTNRLAP---YQFLTAFSQLISRICHSHDEvfvvlmeIIAKVFLAYPQQAMWMMTAVSKSSYPMRVNRCKEILT 2199
Cdd:COG5032  1621 LELSDENIRIAYPllhLLFEPILAQLLSRLSSENNK-------ISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIK 1693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2200 KAihMKKSLEKFVGDATRLtDKLLELCNKSV----DGSNSTLSMSTHFKMLKRLvEDPTFSEILIPLQSVMIPTLPsvlg 2275
Cdd:COG5032  1694 KS--PRKIRKKFKIDISLL-NLSRKLYISVLrsirKRLKRLLELRLKKVSPKLL-LFHAFLEIKLPGQYLLDKPFV---- 1765

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2276 ahanhdpfpghwaYLAGFDDVVEILSS-LQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRR 2354
Cdd:COG5032  1766 -------------LIERFEPEVSVVKShLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRR 1832

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2355 RELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYMTGKELRQCMLpKSAALSEKLKVFqELLLPRHPPVFH 2434
Cdd:COG5032  1833 RDLWIRPYKVIPLSPGSGIIEWVPNSDTLHSILREYHKRKNISIDQEKKLAARL-DNLKLLLKDEFF-TKATLKSPPVLY 1910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2435 EWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDF-NCLFNKGETFEVPEIVPFRLT 2513
Cdd:COG5032  1911 DWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFgFILFNAPGRFPFPEKVPFRLT 1990

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2514 HNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSKpVKGHSKAPLNETgevvnekakTHVLDIE 2593
Cdd:COG5032  1991 RNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRR-LPCFREIQNNEI---------VNVLERF 2060

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 189339266 2594 QR-LQGviktRNRVTGLPLSIEGHVHYLIQEATDENLLCQMYLGWTPYM 2641
Cdd:COG5032  2061 RLkLSE----KDAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPFW 2105
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 2290-2563 1.09e-78

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: 262.03  E-value: 1.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKIYKEKGVYMTgKELRqCMLPKSAA-----LSEKLKVFQELLlpRHPP------VFheWfL 2438
Cdd:cd05169    81 NSGLIGWVPGCDTLHSLIRDYREKRKIPLN-IEHR-LMLQMAPDydnltLIQKVEVFEYAL--ENTPgddlrrVL--W-L 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2439 RTfPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFnclfnkGETFEV-------PEIVPFR 2511
Cdd:cd05169   154 KS-PSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDF------GDCFEVamhrekfPEKVPFR 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 189339266 2512 LTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWS 2563
Cdd:cd05169   227 LTRMLVNAMEVSGVEGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISWR 278
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 2290-2564 4.80e-78

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: 261.42  E-value: 4.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKIYKEKGVYMTGKELR----QCMLPK---------SAALSEK----------------LKV 2420
Cdd:cd05170    81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDsgstPPPVPRpselfynklKPALKAAgirkstsrrewplevlRQV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2421 FQELLLPRHPPVFH-EWFLRTfPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKG 2499
Cdd:cd05170   161 LEELVAETPRDLLArELWCSS-PSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFEKG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189339266 2500 ETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSK 2564
Cdd:cd05170   240 KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDWTA 304
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 2322-2563 4.30e-70

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 236.07  E-value: 4.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2322 MCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRelhIRTYAVIPLNDECGIIEWVNNTAGLRPILTKiYKEKGVYMTGk 2401
Cdd:pfam00454    5 IYKVGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDE-YGENGVPPTA- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2402 eLRQCMLPKSAALSEKLKVFQELLLPRhPPVFHEWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFD 2481
Cdd:pfam00454   80 -MVKILHSALNYPKLKLEFESRISLPP-KVGLLQWFVKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  2482 SFTGECVHVDFN-CLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLRLMRDQREPLMSVLKTFLHDPLV 2560
Cdd:pfam00454  158 KTTGKLFHIDFGlCLPDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLP 237


                   ...
gi 189339266  2561 EWS 2563
Cdd:pfam00454  238 DWS 240
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 2290-2564 2.71e-64

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: 218.98  E-value: 2.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2290 LAGFDDVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLND 2369
Cdd:cd05172     1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2370 ECGIIEWVNNTAGLRPILTKiykekgvymtgkelrqcmlpksaalseklkvfqelllprhpPVFHEWFLRTFPDPTSWYS 2449
Cdd:cd05172    81 RLGLIEWVDNTTPLKEILEN-----------------------------------------DLLRRALLSLASSPEAFLA 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2450 SRSAYCRSTAVMSMVGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGETF-EVPEIVPFRLTHNMVNGMGPMGTEGL 2528
Cdd:cd05172   120 LRSNFARSLAAMSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFGSATQFlPIPELVPFRLTRQLLNLLQPLDARGL 199

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 189339266 2529 FRRACEVTLRLMRDQREPLMSVLKTFLHDPLVEWSK 2564
Cdd:cd05172   200 LRSDMVHVLRALRAGRDLLLATMDVFVKEPLLDWQK 235
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1771-2092 9.21e-56

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


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 198.73  E-value: 9.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1771 NTYRVEAAWKLSQWDLVENYLAADgKSTTWSVRLGQLLLSAKKRDTTTFYDTLKLVRAEQIVPLSAASFErgSYQRGYEF 1850
Cdd:pfam02259    1 APLAAEAAWRLGQWDLMREYLSLM-KKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGE--SYNRAYPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1851 IVRLHMLCELEHSLKPLFRKSPGDSCNEDSL-NWGARLEMTQNSYRAKEPILALRRALLSLNKRPDYNEMVGECWLQSAR 1929
Cdd:pfam02259   78 LVRLQQLAELEEIIQYKQKLGQSSEELKSLLqTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDVYLGGYHAEMWLKFAN 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1930 VARKAGHHQTAYNALLNAGESR----LAELYVERAKWLWSKGDVHQALIVLQKGVELCFPENKSPS-----------ESK 1994
Cdd:pfam02259  158 LARKSGRFSLAEKALLKLLGEDpeewLPEVVYAYAKYLWPTGEQQEALLKLREFLSCYLQKNGELLsglevinptnlEEF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1995 HMLIhGRATLLVGRFMEET----ANFESNAVMKKYKDVTLFLPEWEDGHFYLAKYYDKLMPMVTDNKMEK-QGDLIRYIV 2069
Cdd:pfam02259  238 TELL-ARCYLLKGKWQAALgqnwAEEKSEEILQAYLLATQFDPSWYKAWHTWALFNFEVLRKEEQGKEEEgPEDLSRYVV 316

                          330       340
                   ....*....|....*....|....*.
gi 189339266  2070 L---HFGRSLQYGNQFIYQSMPRMLS 2092
Cdd:pfam02259  317 PaveGYLRSLSLSSENSLQDTLRLLT 342
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 2295-2557 9.56e-38

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: 142.09  E-value: 9.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2295 DVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDaesrRRELHIRTYAVIPLNDECGII 2374
Cdd:cd00142     6 GILKVIHSKQRPKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSILEKE----SVNLVLPPYKVIPLSENSGLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2375 EWVNNTAGLrpiltkiykekgvymtgkelrqcmlpksaalseklkvfQELLlprhppvfhEWFLRTFPDPTSWYSSRSAY 2454
Cdd:cd00142    82 EIVKDAQTI--------------------------------------EDLL---------KSLWRKSPSSQSWLNRRENF 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2455 CRSTAVMSMVGYILGLGDRHGENILFDSfTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACE 2534
Cdd:cd00142   115 SCSLAGYSVLGYIFGIGDRHPSNIMIEP-SGNIFHIDFGFIFSGRKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMV 193

                         250       260
                  ....*....|....*....|...
gi 189339266 2535 VTLRLMRDQREPLMSVLKTFLHD 2557
Cdd:cd00142   194 KIMEILREHADLIVPILEHSLRD 216
UME smart00802
Domain in UVSB PI-3 kinase, MEI-41 and ESR-1; Characteristic domain in UVSP PI-3 kinase, ...
 1119-1225 1.02e-31

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


Pssm-ID: 214825  Cd Length: 107  Bit Score: 120.77  E-value: 1.02e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266   1119 MADYLQPKLLGILAFFNMQLLSSS--VGIEDKKMALTSLMSLMKLMGpKHVSSVRVKMMTTLRTGLRfKDDFPELCCRAW 1196
Cdd:smart00802    1 LADFLKDHFLGILAVFSNILHDSSgkKPYNEKKRALRSIGFLIKLMG-KHISSALPQIMACLQSALE-IPELRSLALRCW 78

                            90       100
                    ....*....|....*....|....*....
gi 189339266   1197 DCFVRCLDHAYLGPLLSHVIVALLPLIHM 1225
Cdd:smart00802   79 HVLIKTLKEEELGPLLDQIFAAILPLWPT 107
UME pfam08064
UME (NUC010) domain; This domain is characteriztic of UVSB PI-3 kinase, MEI-41 and ESR1.
 1122-1223 4.74e-27

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


Pssm-ID: 462350  Cd Length: 102  Bit Score: 107.19  E-value: 4.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266  1122 YLQPKLLGILAFFNMQLLSSSV--GIEDKKMALTSLMSLMKLMGPkHVSSVRVKMMTTLRTGLRfKDDFPELCCRAWDCF 1199
Cdd:pfam08064    1 FLENHILGILARFSDVLNDLRGkkPVEEKKRALRSIEELIKLMGS-AISSALPQIMACLQSALE-IPELREVALSCWDAF 78

                           90       100
                   ....*....|....*....|....
gi 189339266  1200 VRCLDHAYLGPLLSHVIVALLPLI 1223
Cdd:pfam08064   79 VKTLDEEDLGPLLDQTFAAILQLW 102
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
 2307-2564 1.86e-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: 102.22  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2307 KKISLKGSDGK---FYIMMCKPKDdLRKDCRLMEFNSLINKSLRKDAESRRRELHIRTYAVIPLNDECGIIEwvNNTAGL 2383
Cdd:cd05163    19 RRLTIRGHDGSkypFLVQTPSARH-SRREERVMQLFRLLNRVLERKKETRRRNLQFHVPIVVPLSPQVRLVE--DDPSYI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2384 RpiLTKIYKEKGVYmtgKELRQCMLPKSaalseklkvfqelllprhppVFHEWFLRTFPDPTSWYSSRSAYCRSTAVMSM 2463
Cdd:cd05163    96 S--LQDIYEKLEIL---NEIQSKMVPET--------------------ILSNYFLRTMPSPSDLWLFRKQFTLQLALSSF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2464 VGYILGLGDRHGENILFDSFTGECVHVDFNCLFNKGE-TFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTLR-LMR 2541
Cdd:cd05163   151 MTYVLSLGNRTPHRILISRSTGNVFMTDFLPSINSQGpLLDNNEPVPFRLTPNIQHFIGPIGVEGLLTSSMMAIARaLTE 230

                         250       260
                  ....*....|....*....|...
gi 189339266 2542 DQREpLMSVLKTFLHDPLVEWSK 2564
Cdd:cd05163   231 PEYD-LEQYLSLFVRDELISWHK 252
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2214-2533 4.49e-18

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: 88.36  E-value: 4.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2214 DATRLTDKLLELCnKSVDGSNStlsmSTHFKM--LKRLVEDPTFSEILIPlQSVMIPTLPSVlgahanhdpfpghwaYLA 2291
Cdd:cd00896     6 RQQEFVDRLRSLM-KEVKNEKG----SRDKKIerLRELLSDSELGLLLFF-EPLPLPLDPSV---------------KVT 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2292 GFD-DVVEILSSLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDaesrRRELHIRTYAVIPLNDE 2370
Cdd:cd00896    65 GIIpEKSTVFKSALMPLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKE----NLDLKLTPYKVLATSPN 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2371 CGIIEWVNNTAGLRPILTKiykekgvymtGKELRQcmlpksaalseklkvfqelllprhppvfhewFLRTF-PDPTSWYS 2449
Cdd:cd00896   141 DGLVEFVPNSKALADILKK----------YGSILN-------------------------------FLRKHnPDESGPYG 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2450 SRSA----YCRSTAVMSMVGYILGLGDRHGENILFDSfTGECVHVDFNCLFNKGETFEVPeivPFRLTHNMVNGMGPMGT 2525
Cdd:cd00896   180 IKPEvmdnFVKSCAGYCVITYILGVGDRHLDNLLLTK-DGHLFHIDFGYILGRDPKPFPP---PMKLCKEMVEAMGGANS 255

                         330
                  ....*....|
gi 189339266 2526 EG--LFRRAC 2533
Cdd:cd00896   256 EGykEFKKYC 265
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2301-2556 2.51e-16

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: 83.11  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2301 SSLQKPKKISLKGSD--GKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDaesrRRELHIRTYAVIPLNDECGIIEWVN 2378
Cdd:cd05166    71 NSNALPLKLVFRNADprAEPISVIFKVGDDLRQDMLTLQLIRIMDKIWLQE----GLDLKMITFRCVPTGNKRGMVELVP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2379 NTAGLRpiltKIYKEKGVymTGkelrqcmlpksaalseklkVFQELLLprhppvfHEWFLRTFPDPTSWYSSRSAYCRST 2458
Cdd:cd05166   147 EAETLR----EIQTEHGL--TG-------------------SFKDRPL-------ADWLQKHNPSELEYEKAVENFIRSC 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2459 AVMSMVGYILGLGDRHGENILFdSFTGECVHVDFNCLFNKGETFeVP---EIVPFRLTHNMV----NGMGPMGTEGLFRR 2531
Cdd:cd05166   195 AGYCVATYVLGICDRHNDNIML-KTSGHLFHIDFGKFLGDAQMF-GNfkrDRVPFVLTSDMAyvinGGDKPSSRFQLFVD 272

                         250       260
                  ....*....|....*....|....*
gi 189339266 2532 ACEVTLRLMRDQREPLMSVLKTFLH 2556
Cdd:cd05166   273 LCCQAFNIIRKNSNLLLNLLSLMLS 297
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 2324-2538 2.24e-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: 70.70  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2324 KPKDDLRKDCRLMEFNSL---INKSLRKDaesrrreLHIRTYAVIPLNDECGIIEWVNNTAGLRPIltkiykekgvymtG 2400
Cdd:cd05167    55 KVGDDCRQDMLALQLISLfknIFEEVGLD-------LYLFPYRVVATGPGCGVIEVIPNSKSRDQI-------------G 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2401 KELRQCMlpksaalseklkvfqelllprhppvfHEWFLRTFPDP--TSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENI 2478
Cdd:cd05167   115 RETDNGL--------------------------YEYFLSKYGDEstPAFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNI 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189339266 2479 LFDSfTGECVHVDFNCLF------NKGetFEVPeivPFRLTHNMVNGMGPMGTEGLFRRACEVTLR 2538
Cdd:cd05167   169 MIDD-DGHIIHIDFGFIFeispggNLG--FESA---PFKLTKEMVDLMGGSMESEPFKWFVELCVR 228
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
 2610-2641 3.29e-12

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


Pssm-ID: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 62.78  E-value: 3.29e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 189339266  2610 PLSIEGHVHYLIQEATDENLLCQMYLGWTPYM 2641
Cdd:pfam02260    1 PLSVEGQVDELIQEATDPENLAQMYIGWCPWW 32
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2299-2534 1.70e-11

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: 68.37  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2299 ILSSLQKPKKISLKGSD--GKFYIMMCKPKDDLRKDC------RLMEfNSLINKSLrkdaesrrrELHIRTYAVIPLNDE 2370
Cdd:cd00891    66 VMDSKKLPLWLVFKNADpgGDPIKVIFKAGDDLRQDQltlqllRIMD-KLWKKEGL---------DLRMTPYKCIATGDE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2371 CGIIEWVNN---TAglrpiltKIYKEKGVymtgkelrqcmlpKSAALSEKlkvfqelllprhppVFHEWFLRTFPDPTSW 2447
Cdd:cd00891   136 VGMIEVVPNsetTA-------AIQKKYGG-------------FGAAFKDT--------------PISNWLKKHNPTEEEY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2448 -------YSSRSAYCRSTavmsmvgYILGLGDRHGENILFDSfTGECVHVDF-NCLFNKGETFEVP-EIVPFRLTHNMVN 2518
Cdd:cd00891   182 eeavenfIRSCAGYCVAT-------YVLGIGDRHNDNIMVTK-SGHLFHIDFgHFLGNFKKKFGIKrERAPFVFTPEMAY 253

                         250
                  ....*....|....*..
gi 189339266 2519 GMGpmGTEGL-FRRACE 2534
Cdd:cd00891   254 VMG--GEDSEnFQKFED 268
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 2357-2521 1.31e-08

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: 58.81  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2357 LHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGvymtgkelrqcmlpksaalseklkvFQELLlprhppvfhEW 2436
Cdd:cd00893    62 LWLRPYEILSLGPDSGIIEMIKNAVSIDSLKKKLDSFNK-------------------------FVSLS---------DF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2437 FLRTFPDPtSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSfTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNM 2516
Cdd:cd00893   108 FDDNFGDE-AIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDK-EGHIIHIDFGFFLSSHPGFYGFEGAPFKLSSEY 185


                  ....*
gi 189339266 2517 VNGMG 2521
Cdd:cd00893   186 IEVLG 190
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 2357-2533 3.54e-07

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: 54.41  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2357 LHIRTYAVIPLNDECGIIEWVNNTAGLRPIltkiyKEKGVYMTGkeLRQCmlpksaalseklkvfqelllprhppvfhew 2436
Cdd:cd05168    65 LWLRPYEILVTSSDSGLIETIPDTVSIDSL-----KKRFPNFTS--LLDY------------------------------ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2437 FLRTFPDPTS--WYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSfTGECVHVDFN-CLFN--KGETFEVpeiVPFR 2511
Cdd:cd05168   108 FERTFGDPNSerFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDS-EGHIIHIDFGfMLSNspGGLGFET---APFK 183

                         170       180
                  ....*....|....*....|....
gi 189339266 2512 LTHNMVNGMGPMGTEG--LFRRAC 2533
Cdd:cd05168   184 LTQEYVEVMGGLESDMfrYFKTLM 207
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 2324-2541 9.84e-07

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: 53.81  E-value: 9.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2324 KPKDDLRKDCRLMEFNSLINkSLRKDAEsrrRELHIRTYAVIPLNDECGIIEWVNNTAGLRPIltkiykekgvymtgkEL 2403
Cdd:cd05173   100 KNGDDLRQDMLTLQILRLMD-TLWKEAG---LDLRIVPYGCLATGDRSGLIEVVSSAETIADI---------------QL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2404 RQCMLPKSAALSEKlkVFQELLLPRHPPVFHEWFLRTFPdptswySSRSAYCRSTavmsmvgYILGLGDRHGENILFDSf 2483
Cdd:cd05173   161 NSSNVAAAAAFNKD--ALLNWLKEYNSGDDLERAIEEFT------LSCAGYCVAT-------YVLGIGDRHSDNIMVRK- 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189339266 2484 TGECVHVDF-NCLFNKGETFEVP-EIVPFRLTHNMVNGM--GPMG-TE--GLFRRACEVTLRLMR 2541
Cdd:cd05173   225 NGQLFHIDFgHILGNFKSKFGIKrERVPFILTYDFIHVIqqGKTGnTEkfGRFRQYCEDAYLILR 289
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2244-2543 2.19e-06

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: 52.64  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2244 KMLKRLVEDPTFSEILIPLQSvmiPTLPSV-LGAHANHDpfpghwaylagfddvVEILSSLQKPKKISLKGSD-----GK 2317
Cdd:cd05165    33 KLLKECLKQKFYDEALQNFQS---PLNPSHkLGELIIEK---------------CKVMDSKKRPLWLVFENADplalsGE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2318 FYIMMCKPKDDLRKD------CRLMEfnsLINKSLRKDaesrrreLHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIY 2391
Cdd:cd05165    95 DIKIIFKNGDDLRQDmltlqiIRIMD---NIWKEEGLD-------LRMLPYGCLSTGDNVGLIEVVRNAKTIANIQKKKG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2392 KekgvymtgkelRQCMLPKSAALSEKLKvfqelllpRHPPVfHEWFLR---TFPdptswySSRSAYCRSTavmsmvgYIL 2468
Cdd:cd05165   165 K-----------VATLAFNKDSLHKWLK--------EKNKT-GEKYDRaieEFT------LSCAGYCVAT-------YVL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2469 GLGDRHGENILFDSfTGECVHVDF-NCLFNKGETFEVP-EIVPFRLTHNMV----NGMGPMGTEGL--FRRACEVTLRLM 2540
Cdd:cd05165   212 GIGDRHSDNIMVKE-NGQLFHIDFgHFLGNFKKKFGIKrERVPFVLTHDFVyviaRGQDNTKSEEFqeFQELCEKAYLIL 290


                  ...
gi 189339266 2541 RDQ 2543
Cdd:cd05165   291 RRH 293
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 2244-2541 1.26e-05

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: 50.05  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2244 KMLKRLVEDPTFSEILIPLQSvmiPTLPSVLGAHANHDPfpghwaylagfddvVEILSSLQKPKKISLK----GSDGKFY 2319
Cdd:cd05174    38 EMMHVCMKQETYMEALSHLQS---PLDPSIILEEVCVDQ--------------CTFMDSKMKPLWIMYSseeaGAGNVGI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2320 IMmcKPKDDLRKDCRLMEFNSLINKSLRKDAesrrRELHIRTYAVIPLNDECGIIEWVNNTAGLRPIltkiykekgvymt 2399
Cdd:cd05174   101 IF--KNGDDLRQDMLTLQMIQLMDVLWKQEG----LDLRMTPYGCLSTGDKTGLIEVVLHSDTIANI------------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2400 gkELRQCMLPKSAALSEKlkVFQELLLPRHPPVFHEWFLRTFPdptswySSRSAYCRSTavmsmvgYILGLGDRHGENIL 2479
Cdd:cd05174   162 --QLNKSNMAATAAFNKD--ALLNWLKSKNPGDALDQAIEEFT------LSCAGYCVAT-------YVLGIGDRHSDNIM 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189339266 2480 FDSfTGECVHVDF-NCLFNKGETFEVP-EIVPFRLTHNMVNGMGPMGTEG-----LFRRACEVTLRLMR 2541
Cdd:cd05174   225 IRE-SGQLFHIDFgHFLGNFKTKFGINrERVPFILTYDFVHVIQQGKTNNsekfeRFRGYCERAYTILR 292
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 2300-2561 2.17e-05

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: 49.21  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2300 LSSLQKPKKISLKGSD--GKFYIMMCKPKDDLRKDCRLMEFNSLINKSLRKDAesrrRELHIRTYAVIPLNDECGIIEWV 2377
Cdd:cd05176    70 FSSNAVPLKVALVNADplGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLQEG----LDLRMVIFKCLSTGKDRGMVELV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2378 NNTAGLRpiltKIYKEKGVymTGKelrqcmlpksaalseklkvFQELLLPrhppvfhEWFLRTFPDPTSWYSSRSAYCRS 2457
Cdd:cd05176   146 PSSDTLR----KIQVEYGV--TGS-------------------FKDKPLA-------EWLRKYNPSEEEYEKASENFIYS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2458 TAVMSMVGYILGLGDRHGENILFDSfTGECVHVDFNCLFNKGETFEV--PEIVPFRLTHNMV----NGMGPMGTEGLFRR 2531
Cdd:cd05176   194 CAGCCVATYVLGICDRHNDNIMLRS-TGHMFHIDFGKFLGHAQMFGSfkRDRAPFVLTSDMAyvinGGEKPTIRFQLFVD 272

                         250       260       270
                  ....*....|....*....|....*....|
gi 189339266 2532 ACEVTLRLMRDQREPLMSVLKTFLHDPLVE 2561
Cdd:cd05176   273 LCCQAYNLIRKHTNLFLNLLSLMLSSGLPE 302
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 2324-2524 1.34e-03

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: 43.70  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2324 KPKDDLRKDCRLMEfnslINKSLRKDAESRRRELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKIYKEKGVYmtgkel 2403
Cdd:cd00894   105 KHGDDLRQDMLILQ----ILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAF------ 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 2404 rqcmlpKSAALSEKLK---VFQElllprhppvfhewflRTFPDPTSWYSSRSAYCRSTavmsmvgYILGLGDRHGENILF 2480
Cdd:cd00894   175 ------KDEVLNHWLKekcPIEE---------------KFQAAVERFVYSCAGYCVAT-------FVLGIGDRHNDNIMI 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 189339266 2481 dSFTGECVHVDFNCLFNKGETFE--VPEIVPFRLTHNMVNGMGPMG 2524
Cdd:cd00894   227 -TETGNLFHIDFGHILGNYKSFLgiNKERVPFVLTPDFLFVMGTSG 271
NR_LBD_Lrh-1 cd07069
The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor ...
 1529-1607 1.86e-03

The ligand binding domain of the liver receptor homolog-1, a member of nuclear receptor superfamily,; The ligand binding domain (LBD) of the liver receptor homolog-1 (LRH-1): LRH-1 belongs to nuclear hormone receptor superfamily, and is expressed mainly in the liver, intestine, exocrine pancreas, and ovary. Most nuclear receptors function as homodimer or heterodimers. However, LRH-1 binds DNA as a monomer, and is a regulator of bile-acid homeostasis, steroidogenesis, reverse cholesterol transport and the initial stages of embryonic development. Recently, phospholipids have been identified as potential ligand for LRH-1 and steroidogenic factor-1 (SF-1). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, LRH-1 has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 132754 [Multi-domain]  Cd Length: 241  Bit Score: 42.71  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189339266 1529 LPHILVYvLLGCnQEDQQEVYAEIMAVLKHdEQHAISTQDSASD---LCQLSTQTVFSVLdhltQWARHK--FQALNAE- 1602
Cdd:cd07069     1 IPHLILE-LLKC-EPDEPQVQAKIMAYLQQ-EQANRSKHEKLSTfglMCKMADQTLFSIV----EWARSSifFRELKVDd 73


                  ....*..
gi 189339266 1603 --KLAQN 1607
Cdd:cd07069    74 qmKLLQN 80
 
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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