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Conserved domains on  [gi|4050084|gb|AAD11941|]
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mitotic checkpoint protein kinase BUB1B [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 750-1045 0e+00

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: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   750 MPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNS----AELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSC 825
Cdd:cd14029    1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   826 YQ----YQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCN 901
Cdd:cd14029   81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSSSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   902 KNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLS 981
Cdd:cd14029  161 ELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKIS 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4050084   982 QNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPG 1045
Cdd:cd14029  241 QNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
 57-179 3.64e-57

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: 192.74  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084      57 QQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPL 136
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4050084     137 DMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGI 179
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
PTZ00121 super family cl31754
MAEBL; Provisional
 369-488 2.91e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    369 RKPGKEEGDPLQRVQSHQQASEEKK-EKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLT----SAEKRAEMQ 443
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKkkaeEAKKKADAA 1334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 4050084    444 KQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQK 488
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
 
Name Accession Description Interval E-value
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 750-1045 0e+00

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: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   750 MPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNS----AELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSC 825
Cdd:cd14029    1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   826 YQ----YQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCN 901
Cdd:cd14029   81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSSSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   902 KNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLS 981
Cdd:cd14029  161 ELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKIS 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4050084   982 QNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPG 1045
Cdd:cd14029  241 QNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
 57-179 3.64e-57

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: 192.74  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084      57 QQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPL 136
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4050084     137 DMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGI 179
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
 56-178 7.18e-56

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: 188.97  E-value: 7.18e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084       56 QQQKRAFEYEIR-FYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNE 134
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGGKESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 4050084      135 PLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEG 178
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
PRK14879 PRK14879
Kae1-associated kinase Bud32;
837-920 3.98e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 46.05  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    837 QYINCFTLQDLLQHSEYITHEItvliIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRihDPYdcnknnqalkIVDF---- 912
Cdd:PRK14879   79 EYIEGEPLKDLINSNGMEELEL----SREIGRLVGKLHSAGIIHGDLTTSNMILSGG--KIY----------LIDFglae 142

                          90
                  ....*....|....
gi 4050084    913 ------SYSVDLRV 920
Cdd:PRK14879  143 fskdleDRAVDLHV 156
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 837-920 1.04e-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: 44.51  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084     837 QYINCFTLQDLLqhSEYITHeitvlIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRihDPYdcnknnqalkIVDFS--- 913
Cdd:TIGR03724   77 EYIEGKPLKDVI--EENGDE-----LAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD--KVY----------LIDFGlgk 137

                           90
                   ....*....|....
gi 4050084     914 -------YSVDLRV 920
Cdd:TIGR03724  138 ysdeiedKAVDLHV 151
PTZ00121 PTZ00121
MAEBL; Provisional
 369-488 2.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    369 RKPGKEEGDPLQRVQSHQQASEEKK-EKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLT----SAEKRAEMQ 443
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKkkaeEAKKKADAA 1334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 4050084    444 KQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQK 488
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 373-492 2.57e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084     373 KEEGDPLQRVQSHQQASEEK-KEKMMYCKEKIyagvgefsFEEIRAEVFRKKLKEQREAE-------LLTSAEKRAEMQK 444
Cdd:pfam15709  354 RREQEEQRRLQQEQLERAEKmREELELEQQRR--------FEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQ 425

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 4050084     445 qiEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGM 492
Cdd:pfam15709  426 --EEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 826-920 8.30e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 38.02  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   826 YQYQDGCIVwHQYINCFTLQDLLQhseyiTHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILrnrihdpydcnkNNQ 905
Cdd:COG3642   26 VDPDDADLV-MEYIEGETLADLLE-----EGELPPELLRELGRLLARLHRAGIVHGDLTTSNILV------------DDG 87

                         90       100
                 ....*....|....*....|....*
gi 4050084   906 ALKIVDFSYS----------VDLRV 920
Cdd:COG3642   88 GVYLIDFGLArysdpledkaVDLAV 112
 
Name Accession Description Interval E-value
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 750-1045 0e+00

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: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   750 MPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNS----AELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSC 825
Cdd:cd14029    1 MPDLEEEKEIELGNETYCIKREYILHENYKLFMGAPVNWdmeeAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   826 YQ----YQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCN 901
Cdd:cd14029   81 QTncflYQNGCISLHKDINRFTLQDILLDSEEIIKEVIVLVTYNLLSLVEKLHKAEIVHGDLRPETLLLDDRIFDPSSSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   902 KNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLS 981
Cdd:cd14029  161 ELEGALKIVDFSHSMDLRLQPTVSSLRGFPIAQSESGQQFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKIS 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4050084   982 QNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPG 1045
Cdd:cd14029  241 QNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRELKGEMMELFDSGFQDKLCNYLIQLGMRLNPL 304
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
 57-179 3.64e-57

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: 192.74  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084      57 QQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPL 136
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGGKESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4050084     137 DMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGI 179
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
 56-178 7.18e-56

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: 188.97  E-value: 7.18e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084       56 QQQKRAFEYEIR-FYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNE 134
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGGKESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 4050084      135 PLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEG 178
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
 752-1043 4.41e-45

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: 164.84  E-value: 4.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   752 KLEIEKEieLGNEDYCIKREY---LICEDYKLFwvaprnsaeltVIKVSSQPVPWDFYINLKLKERLN-----EDFDHFC 823
Cdd:cd13981    1 TYVISKE--LGEGGYASVYLAkddDEQSDGSLV-----------ALKVEKPPSIWEFYICDQLHSRLKnsrlrESISGAH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   824 SCYQYQDGCIVWHQYINCFTLQDLL----QHSEYITHE-ITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPY 898
Cdd:cd13981   68 SAHLFQDESILVMDYSSQGTLLDVVnkmkNKTGGGMDEpLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICADW 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   899 ----DCNKNNQALKIVDFSYSVDLRVQLD------VFTLSGFRTVQILEGQkilancSSPYQVDLFGIADLAHLLLFKEH 968
Cdd:cd13981  148 pgegENGWLSKGLKLIDFGRSIDMSLFPKnqsfkaDWHTDSFDCIEMREGR------PWTYQIDYFGIAATIHVMLFGKY 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4050084   969 LQV-FWDGSfWKLSQNISELKDGELWNKFFVRILNANDEA-TVSVLGELAAEMNGVfDTTFQSHLNKALWKVGKLTS 1043
Cdd:cd13981  222 MELtQESGR-WKINQNLKRYWQRDIWNKFFDTLLNPEPSCnTLPLLEELRKILEEM-EAWFEASLCNNLVVLRKLRE 296
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 785-1031 2.56e-27

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: 113.02  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   785 PRNSAELtVIKVSSQPVPWDFYINLKLKERLNED----FDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEI-- 858
Cdd:cd14028   27 AKSNQKF-VLKVQKPANPWEFYIGTQLMERLKPSmrhlFIKFYSAHLFQNGSVLVGELYNYGTLLNAINLYKKLPEKVmp 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   859 TVLIIY---NLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNN--QALKIVDFSYSVDLRVQLD--VFT----L 927
Cdd:cd14028  106 QPLVIYfamRILYMVEQLHDCEIIHGDIKPDNFILGERFLENDDCEEDDlsHGLALIDLGQSIDMKLFPKgtAFTakceT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   928 SGFRTVQILEGQKilanCSspYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEA 1007
Cdd:cd14028  186 SGFQCTEMLSNKP----WN--YQTDYFGVAATVYCMLFGTYMKVKNEGGVWKPEGSFRRLPHLELWNEFFHVMLNIPDCH 259

                        250       260
                 ....*....|....*....|....
gi 4050084  1008 TVSVLGELAAEMNGVFDTTFQSHL 1031
Cdd:cd14028  260 SLPSLDALREKLKKVFQQHYTNKI 283
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 793-963 4.56e-06

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: 48.81  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   793 VIKVSSQPVPwDFYINLKLKE-RLNEDFDH-----FCSCYQYQDG-CIVWhQYINCFTLQDLL-QHSEYITHEITVLIIY 864
Cdd:cd00180   22 AVKVIPKEKL-KKLLEELLREiEILKKLNHpnivkLYDVFETENFlYLVM-EYCEGGSLKDLLkENKGPLSEEEALSILR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   865 NLLTIVEMLHKAEIVHGDLSPR-CLILRNRIhdpydcnknnqaLKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILA 943
Cdd:cd00180  100 QLLSALEYLHSNGIIHRDLKPEnILLDSDGT------------VKLADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELLG 167

                        170       180
                 ....*....|....*....|....*..
gi 4050084   944 NCSSPYQVDLFG-------IADLAHLL 963
Cdd:cd00180  168 GRYYGPKVDIWSlgvilyeLEELKDLI 194
PRK14879 PRK14879
Kae1-associated kinase Bud32;
837-920 3.98e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 46.05  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    837 QYINCFTLQDLLQHSEYITHEItvliIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRihDPYdcnknnqalkIVDF---- 912
Cdd:PRK14879   79 EYIEGEPLKDLINSNGMEELEL----SREIGRLVGKLHSAGIIHGDLTTSNMILSGG--KIY----------LIDFglae 142

                          90
                  ....*....|....
gi 4050084    913 ------SYSVDLRV 920
Cdd:PRK14879  143 fskdleDRAVDLHV 156
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 837-920 1.04e-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: 44.51  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084     837 QYINCFTLQDLLqhSEYITHeitvlIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRihDPYdcnknnqalkIVDFS--- 913
Cdd:TIGR03724   77 EYIEGKPLKDVI--EENGDE-----LAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD--KVY----------LIDFGlgk 137

                           90
                   ....*....|....
gi 4050084     914 -------YSVDLRV 920
Cdd:TIGR03724  138 ysdeiedKAVDLHV 151
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 842-948 2.12e-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: 44.52  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   842 FTLQDLLQHSE---YITHEITVL------IIYNLLTIVEMLHKAEIVHGDLSPRCLILrnrihdpydcnKNNQALKIVDF 912
Cdd:cd14182   86 FLVFDLMKKGElfdYLTEKVTLSeketrkIMRALLEVICALHKLNIVHRDLKPENILL-----------DDDMNIKLTDF 154

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 4050084   913 SYSvdlrvqldvftlsgfrtVQILEGQKILANCSSP 948
Cdd:cd14182  155 GFS-----------------CQLDPGEKLREVCGTP 173
PTZ00121 PTZ00121
MAEBL; Provisional
 369-488 2.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    369 RKPGKEEGDPLQRVQSHQQASEEKK-EKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLT----SAEKRAEMQ 443
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKkkaeEAKKKADAA 1334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 4050084    444 KQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQK 488
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
PTZ00121 PTZ00121
MAEBL; Provisional
 373-488 6.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    373 KEEGDPLQRVQSHQQASEEKKEKmmyCKEKIYAGVGEFSFEEIR-AEVFRKKLKEQREAELLT----SAEKRAEMQKQIE 447
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKKAEEAKkADEAKKKAEEAKKADEAKkkaeEAKKKADEAKKAA 1506

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4050084    448 EMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQK 488
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 811-929 1.47e-03

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 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: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 41.53  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   811 LKERLNEDFdhfCSCYQYQD--GCI-VWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRC 887
Cdd:cd14202   55 LKELKHENI---VALYDFQEiaNSVyLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQN 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 4050084   888 LILRNRihDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSG 929
Cdd:cd14202  132 ILLSYS--GGRKSNPNNIRIKIADFGFARYLQNNMMAATLCG 171
PRK12704 PRK12704
phosphodiesterase; Provisional
 383-463 2.30e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084    383 QSHQQASEEKKEKMMYCKEKIYAGVGEFSFE--EIRAEVFR--KKLK-------------EQREAELLTSAEKRAEMQKQ 445
Cdd:PRK12704   46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrERRNELQKleKRLLqkeenldrklellEKREEELEKKEKELEQKQQE 125

                          90
                  ....*....|....*...
gi 4050084    446 IEEMEKKLKEIQTTQQER 463
Cdd:PRK12704  126 LEKKEEELEELIEEQLQE 143
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
 838-882 2.55e-03

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 41.00  E-value: 2.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4050084    838 YINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGD 882
Cdd:PHA03390   90 YIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHND 134
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 373-492 2.57e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084     373 KEEGDPLQRVQSHQQASEEK-KEKMMYCKEKIyagvgefsFEEIRAEVFRKKLKEQREAE-------LLTSAEKRAEMQK 444
Cdd:pfam15709  354 RREQEEQRRLQQEQLERAEKmREELELEQQRR--------FEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQ 425

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 4050084     445 qiEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGM 492
Cdd:pfam15709  426 --EEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 844-916 3.44e-03

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 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: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 40.61  E-value: 3.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4050084   844 LQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDcnknNQALKIVDFSYSV 916
Cdd:cd14097   87 LKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNND----KLNIKVTDFGLSV 155
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
 832-895 4.12e-03

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 40.47  E-value: 4.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   832 CIVWHQYinCFTLQDL--LQH---SEYITHEI-TVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIH 895
Cdd:cd13974  103 CLCAHDF--SDKTADLinLQHyviREKRLSEReALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR 170
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 826-920 8.30e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 38.02  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4050084   826 YQYQDGCIVwHQYINCFTLQDLLQhseyiTHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILrnrihdpydcnkNNQ 905
Cdd:COG3642   26 VDPDDADLV-MEYIEGETLADLLE-----EGELPPELLRELGRLLARLHRAGIVHGDLTTSNILV------------DDG 87

                         90       100
                 ....*....|....*....|....*
gi 4050084   906 ALKIVDFSYS----------VDLRV 920
Cdd:COG3642   88 GVYLIDFGLArysdpledkaVDLAV 112
 
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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