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Conserved domains on  [gi|568915165|ref|XP_006498685|]
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mitotic checkpoint serine/threonine-protein kinase BUB1 beta isoform X1 [Mus musculus]

Protein Classification

mitotic checkpoint serine/threonine-protein kinase BUB1; choline kinase family protein( domain architecture ID 13746932)

mitotic checkpoint serine/threonine-protein kinase BUB1 (Budding uninhibited by benzimidazoles 1) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment| choline kinase (ChoK) family protein similar to ChoK that catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
740-1036 1.60e-152

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14029:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 304  Bit Score: 455.09  E-value: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  740 MPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSS----AELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSC 815
Cdd:cd14029     1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  816 CQ----YQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDyV 891
Cdd:cd14029    81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSS-S 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  892 NKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKL 971
Cdd:cd14029   160 NELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKI 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915165  972 SQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPE 1036
Cdd:cd14029   240 SQNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
51-173 4.47e-58

Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of the binding of BUB1 and MAD3 to CDC20p.


:

Pssm-ID: 462420  Cd Length: 123  Bit Score: 195.44  E-value: 4.47e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165    51 QQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPL 130
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915165   131 DMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGI 173
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
half-pint super family cl31128
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
253-445 7.20e-04

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


The actual alignment was detected with superfamily member TIGR01645:

Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.52  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   253 NAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAgrrphdnPASVTSIPSVLPS 332
Cdd:TIGR01645  321 AAVLGPRAQSPATPSSSLPTDIGNKAVVSSAKKEAEEVPPLPQAAPAVVKPGPMEIPTPV-------PPPGLAIPSLVAP 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   333 FtpyveesaqqTVMTPCKIEPSInhVLSTRKPGREEGDPLQRVQSHQQ--GCEEKKEKMMYCKEKIYAGVGEFSFEEIRA 410
Cdd:TIGR01645  394 P----------GLVAPTEINPSF--LASPRKKMKREKLPVTFGALDDTlaWKEPSKEDQTSEDGKMLAIMGEAAAALALE 461
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568915165   411 EVFRKKLKERREAELLTSAKKREEMQKQIEEMERR 445
Cdd:TIGR01645  462 PKKKKKEKEGEELQPKLVMNSEDASLASQEGMSIR 496
 
Name Accession Description Interval E-value
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
740-1036 1.60e-152

Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BubR1 (Budding uninhibited by benzimidazoles R1) is also called Bub1 beta (Bub1b). It contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. BubR1 inhibits APC/C through direct binding. It also plays an important role in stabilizing kinetochore-microtubule attachments. Mutant mice expressing only 10% normal BubR1 protein are viable and develop into adult mice, but display many early aging-associated phenotypes including reduced lifespan, muscle atrophy, cataracts, impaired wound healing, and infertility. The BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270931 [Multi-domain]  Cd Length: 304  Bit Score: 455.09  E-value: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  740 MPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSS----AELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSC 815
Cdd:cd14029     1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  816 CQ----YQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDyV 891
Cdd:cd14029    81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSS-S 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  892 NKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKL 971
Cdd:cd14029   160 NELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKI 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915165  972 SQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPE 1036
Cdd:cd14029   240 SQNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
51-173 4.47e-58

Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of the binding of BUB1 and MAD3 to CDC20p.


Pssm-ID: 462420  Cd Length: 123  Bit Score: 195.44  E-value: 4.47e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165    51 QQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPL 130
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915165   131 DMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGI 173
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
50-172 1.09e-57

Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of the binding of BUB1 and MAD3 to CDC20p.


Pssm-ID: 214817  Cd Length: 124  Bit Score: 194.36  E-value: 1.09e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165     50 QQQKRAFESEIR-FYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNE 128
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGGKESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 568915165    129 PLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEG 172
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
PRK14879 PRK14879
Kae1-associated kinase Bud32;
827-911 4.76e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 42.59  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  827 QYINCSTLQNLLQHSEFVTHEIIVLIIYnlltIVEKLHRAEIVHGDLSPRSLILRNRihDPYdyvnkddhavrIMDF--- 903
Cdd:PRK14879   79 EYIEGEPLKDLINSNGMEELELSREIGR----LVGKLHSAGIIHGDLTTSNMILSGG--KIY-----------LIDFgla 141
                          90
                  ....*....|....*
gi 568915165  904 -------SYSVDLRV 911
Cdd:PRK14879  142 efskdleDRAVDLHV 156
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
827-911 5.42e-04

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 42.20  E-value: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   827 QYINCSTLQNLLQhsefvthEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRihDPYdyvnkddhavrIMDFS-- 904
Cdd:TIGR03724   77 EYIEGKPLKDVIE-------ENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD--KVY-----------LIDFGlg 136
                           90
                   ....*....|....*
gi 568915165   905 --------YSVDLRV 911
Cdd:TIGR03724  137 kysdeiedKAVDLHV 151
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
253-445 7.20e-04

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.52  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   253 NAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAgrrphdnPASVTSIPSVLPS 332
Cdd:TIGR01645  321 AAVLGPRAQSPATPSSSLPTDIGNKAVVSSAKKEAEEVPPLPQAAPAVVKPGPMEIPTPV-------PPPGLAIPSLVAP 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   333 FtpyveesaqqTVMTPCKIEPSInhVLSTRKPGREEGDPLQRVQSHQQ--GCEEKKEKMMYCKEKIYAGVGEFSFEEIRA 410
Cdd:TIGR01645  394 P----------GLVAPTEINPSF--LASPRKKMKREKLPVTFGALDDTlaWKEPSKEDQTSEDGKMLAIMGEAAAALALE 461
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568915165   411 EVFRKKLKERREAELLTSAKKREEMQKQIEEMERR 445
Cdd:TIGR01645  462 PKKKKKEKEGEELQPKLVMNSEDASLASQEGMSIR 496
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
827-903 2.91e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.54  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915165  827 QYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRnrihdpydyvnkDDHAVRIMDF 903
Cdd:COG0515    87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT------------PDGRVKLIDF 151
 
Name Accession Description Interval E-value
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
740-1036 1.60e-152

Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BubR1 (Budding uninhibited by benzimidazoles R1) is also called Bub1 beta (Bub1b). It contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. BubR1 inhibits APC/C through direct binding. It also plays an important role in stabilizing kinetochore-microtubule attachments. Mutant mice expressing only 10% normal BubR1 protein are viable and develop into adult mice, but display many early aging-associated phenotypes including reduced lifespan, muscle atrophy, cataracts, impaired wound healing, and infertility. The BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270931 [Multi-domain]  Cd Length: 304  Bit Score: 455.09  E-value: 1.60e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  740 MPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSS----AELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSC 815
Cdd:cd14029     1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  816 CQ----YQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDyV 891
Cdd:cd14029    81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSS-S 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  892 NKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKL 971
Cdd:cd14029   160 NELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKI 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915165  972 SQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPE 1036
Cdd:cd14029   240 SQNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
51-173 4.47e-58

Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of the binding of BUB1 and MAD3 to CDC20p.


Pssm-ID: 462420  Cd Length: 123  Bit Score: 195.44  E-value: 4.47e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165    51 QQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPL 130
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568915165   131 DMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGI 173
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
50-172 1.09e-57

Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of the binding of BUB1 and MAD3 to CDC20p.


Pssm-ID: 214817  Cd Length: 124  Bit Score: 194.36  E-value: 1.09e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165     50 QQQKRAFESEIR-FYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNE 128
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGGKESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 568915165    129 PLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEG 172
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
784-1031 1.49e-33

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 131.32  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  784 IKASSQPIPWDFYINLKLKERLN-----EDYDQLCSCCQYQDGHVVWYQYINCSTLQNLL----QHSEFVTHEIIVL-II 853
Cdd:cd13981    33 LKVEKPPSIWEFYICDQLHSRLKnsrlrESISGAHSAHLFQDESILVMDYSSQGTLLDVVnkmkNKTGGGMDEPLAMfFT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  854 YNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDYVNKDDH---AVRIMDFSYSVDLRVQLD--AFAYSGFRTAQILE 928
Cdd:cd13981   113 IELLKVVEALHEVGIIHGDIKPDNFLLRLEICADWPGEGENGWlskGLKLIDFGRSIDMSLFPKnqSFKADWHTDSFDCI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  929 GQkiLANCSSPYHVDLLGIADLAHLLLFKEHLHV-FWDGLlWKLSQSTSELKDSELWNKFFVRILNASD-KSTVSVLGEL 1006
Cdd:cd13981   193 EM--REGRPWTYQIDYFGIAATIHVMLFGKYMELtQESGR-WKINQNLKRYWQRDIWNKFFDTLLNPEPsCNTLPLLEEL 269
                         250       260
                  ....*....|....*....|....*
gi 568915165 1007 AAEMgGAFDATFHSHLNRALWKLGK 1031
Cdd:cd13981   270 RKIL-EEMEAWFEASLCNNLVVLRK 293
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
792-1006 1.55e-22

Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein Bub1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Bub1 (Budding uninhibited by benzimidazoles 1) contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding, a GLEBS motif for Bub3/kinetochore binding, and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Bub1 contributes to the inhibition of APC/C by phosphorylating its crucial cofactor, Cdc20, rendering it unable to activate APC/C. In addition, Bub1 facilitates the localization to kinetochores of other SAC and motor proteins including Mad1, Mad2, BubR1, and Plk1. It acts as the master organizer of the functional inner centromere. Bub1 also play roles in protecting sister chromatid cohesion and normal metaphase congression. The Bub1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270930 [Multi-domain]  Cd Length: 290  Bit Score: 99.15  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  792 PWDFYINLKLKERLNED----YDQLCSCCQYQDGHVVWYQYINCSTLQNLLQHSEFVTHEII--VLIIY---NLLTIVEK 862
Cdd:cd14028    43 PWEFYIGTQLMERLKPSmrhlFIKFYSAHLFQNGSVLVGELYNYGTLLNAINLYKKLPEKVMpqPLVIYfamRILYMVEQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  863 LHRAEIVHGDLSPRSLILRNRIHDPYDYVNKD-DHAVRIMDFSYSVDLRVQLDAFAY------SGFRTAQILEGQKilan 935
Cdd:cd14028   123 LHDCEIIHGDIKPDNFILGERFLENDDCEEDDlSHGLALIDLGQSIDMKLFPKGTAFtakcetSGFQCTEMLSNKP---- 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915165  936 CSspYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKLSQSTSELKDSELWNKFFVRILNASDKSTVSVLGEL 1006
Cdd:cd14028   199 WN--YQTDYFGVAATVYCMLFGTYMKVKNEGGVWKPEGSFRRLPHLELWNEFFHVMLNIPDCHSLPSLDAL 267
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
811-945 4.42e-05

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 46.75  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  811 QLCSCCQYQDGHVVWYQYINCSTLQNLLQH---SEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRI--- 884
Cdd:cd14157    56 PLLGFCVESDCHCLIYPYMPNGSLQDRLQQqggSHPLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLlpk 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915165  885 --HDPYDYVNKDDHAVRIM---------------DFSYSVDLRVQLDAFAySGFRTAQILEGQKILANCSSP-YHVDLL 945
Cdd:cd14157   136 lgHSGLRLCPVDKKSVYTMmktkvlqislaylpeDFVRHGQLTEKVDIFS-CGVVLAEILTGIKAMDEFRSPvYLKDLL 213
PRK14879 PRK14879
Kae1-associated kinase Bud32;
827-911 4.76e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 42.59  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  827 QYINCSTLQNLLQHSEFVTHEIIVLIIYnlltIVEKLHRAEIVHGDLSPRSLILRNRihDPYdyvnkddhavrIMDF--- 903
Cdd:PRK14879   79 EYIEGEPLKDLINSNGMEELELSREIGR----LVGKLHSAGIIHGDLTTSNMILSGG--KIY-----------LIDFgla 141
                          90
                  ....*....|....*
gi 568915165  904 -------SYSVDLRV 911
Cdd:PRK14879  142 efskdleDRAVDLHV 156
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
852-939 5.22e-04

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 43.37  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  852 IIYNLLTIVEKLHRAEIVHGDLSPRSLILrnrihdpydyvnKDDHAVRIMDFSYSVdlrvqldafaysgfrtaQILEGQK 931
Cdd:cd14182   115 IMRALLEVICALHKLNIVHRDLKPENILL------------DDDMNIKLTDFGFSC-----------------QLDPGEK 165

                  ....*...
gi 568915165  932 ILANCSSP 939
Cdd:cd14182   166 LREVCGTP 173
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
827-911 5.42e-04

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 42.20  E-value: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   827 QYINCSTLQNLLQhsefvthEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRihDPYdyvnkddhavrIMDFS-- 904
Cdd:TIGR03724   77 EYIEGKPLKDVIE-------ENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD--KVY-----------LIDFGlg 136
                           90
                   ....*....|....*
gi 568915165   905 --------YSVDLRV 911
Cdd:TIGR03724  137 kysdeiedKAVDLHV 151
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
253-445 7.20e-04

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.52  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   253 NAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAgrrphdnPASVTSIPSVLPS 332
Cdd:TIGR01645  321 AAVLGPRAQSPATPSSSLPTDIGNKAVVSSAKKEAEEVPPLPQAAPAVVKPGPMEIPTPV-------PPPGLAIPSLVAP 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165   333 FtpyveesaqqTVMTPCKIEPSInhVLSTRKPGREEGDPLQRVQSHQQ--GCEEKKEKMMYCKEKIYAGVGEFSFEEIRA 410
Cdd:TIGR01645  394 P----------GLVAPTEINPSF--LASPRKKMKREKLPVTFGALDDTlaWKEPSKEDQTSEDGKMLAIMGEAAAALALE 461
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568915165   411 EVFRKKLKERREAELLTSAKKREEMQKQIEEMERR 445
Cdd:TIGR01645  462 PKKKKKEKEGEELQPKLVMNSEDASLASQEGMSIR 496
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
827-903 2.91e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.54  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915165  827 QYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRnrihdpydyvnkDDHAVRIMDF 903
Cdd:COG0515    87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT------------PDGRVKLIDF 151
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
811-909 6.47e-03

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 39.18  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  811 QLCSCCQYQDGHVVWYQYINCSTLQNLL-QHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHdpyd 889
Cdd:cd00180    55 KLYDVFETENFLYLVMEYCEGGSLKDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---- 130
                          90       100
                  ....*....|....*....|
gi 568915165  890 yvnkddhaVRIMDFSYSVDL 909
Cdd:cd00180   131 --------VKLADFGLAKDL 142
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
822-910 7.17e-03

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 39.65  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915165  822 HVVWyQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILrnrihdpydYVNKDDHAVRIM 901
Cdd:cd14012    80 YLLT-EYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLL---------DRDAGTGIVKLT 149

                  ....*....
gi 568915165  902 DFSYSVDLR 910
Cdd:cd14012   150 DYSLGKTLL 158
 
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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