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Conserved domains on  [gi|519666801|ref|NP_001265546|]
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mitotic checkpoint serine/threonine-protein kinase BUB1 isoform 3 [Homo sapiens]

Protein Classification

mitotic checkpoint serine/threonine-protein kinase BUB1( domain architecture ID 10654989)

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; contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding

EC:  2.7.11.1
Gene Ontology:  GO:0005524|GO:0006468|GO:0004674|GO:0051301
PubMed:  17643075

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 ...
 786-1016 1.13e-153

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 cd14028:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 290  Bit Score: 456.62  E-value: 1.13e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  786 LVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLV 865
Cdd:cd14028     1 SVYVDHLLGEGAFAQVYQATQLDLNDAKSNQKFVLKVQKPANPWEFYIGTQLMERLKPSMRHLFIKFYSAHLFQNGSVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  866 GELYSYGTLLD-----------------------------------------------------------DEDDLSAGLA 886
Cdd:cd14028    81 GELYNYGTLLNainlykklpekvmpqplviyfamrilymveqlhdceiihgdikpdnfilgerflenddcEEDDLSHGLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  887 LIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLP 966
Cdd:cd14028   161 LIDLGQSIDMKLFPKGTAFTAKCETSGFQCTEMLSNKPWNYQTDYFGVAATVYCMLFGTYMKVKNEGGVWKPEGSFRRLP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 519666801  967 HLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRL 1016
Cdd:cd14028   241 HLELWNEFFHVMLNIPDCHSLPSLDALREKLKKVFQQHYTNKIRALRNRL 290
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
 5-125 1.37e-48

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: 168.17  E-value: 1.37e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801      5 ENVLQMLEAHMQ-SYKGNDPLGEWERYIQWVEENFPEN--KEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSD 81
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGgkESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 519666801     82 LHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRG 125
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
 
Name Accession Description Interval E-value
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 786-1016 1.13e-153

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: 456.62  E-value: 1.13e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  786 LVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLV 865
Cdd:cd14028     1 SVYVDHLLGEGAFAQVYQATQLDLNDAKSNQKFVLKVQKPANPWEFYIGTQLMERLKPSMRHLFIKFYSAHLFQNGSVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  866 GELYSYGTLLD-----------------------------------------------------------DEDDLSAGLA 886
Cdd:cd14028    81 GELYNYGTLLNainlykklpekvmpqplviyfamrilymveqlhdceiihgdikpdnfilgerflenddcEEDDLSHGLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  887 LIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLP 966
Cdd:cd14028   161 LIDLGQSIDMKLFPKGTAFTAKCETSGFQCTEMLSNKPWNYQTDYFGVAATVYCMLFGTYMKVKNEGGVWKPEGSFRRLP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 519666801  967 HLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRL 1016
Cdd:cd14028   241 HLELWNEFFHVMLNIPDCHSLPSLDALREKLKKVFQQHYTNKIRALRNRL 290
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
 5-125 1.37e-48

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: 168.17  E-value: 1.37e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801      5 ENVLQMLEAHMQ-SYKGNDPLGEWERYIQWVEENFPEN--KEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSD 81
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGgkESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 519666801     82 LHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRG 125
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
 6-126 9.60e-46

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: 160.00  E-value: 9.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801     6 NVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPEN--KEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLH 83
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGgkESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 519666801    84 QFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGI 126
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 789-944 1.68e-05

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 47.52  E-value: 1.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801    789 VHHLLGEGAFAQVYEATqgdlnDAKNKQKFVLKVQKPANPWEFYIGT----QLMERLKpsmqHMF-MKFYSAHLFQNGSV 863
Cdd:smart00220    3 ILEKLGEGSFGKVYLAR-----DKKTGKLVAIKVIKKKKIKKDRERIlreiKILKKLK----HPNiVRLYDVFEDEDKLY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801    864 LVGELYSYGTLLD--------DEDD-------LSAGLA--------------------------LIDLGQSidmKLFPKG 902
Cdd:smart00220   74 LVMEYCEGGDLFDllkkrgrlSEDEarfylrqILSALEylhskgivhrdlkpenilldedghvkLADFGLA---RQLDPG 150

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 519666801    903 TIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFG 944
Cdd:smart00220  151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTG 192
Pkinase pfam00069
Protein kinase domain;
789-945 4.15e-04

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 43.00  E-value: 4.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801   789 VHHLLGEGAFAQVYEATqgdlnDAKNKQKFVLKVQKPANPWEFYIGTQLMER--LKpSMQHMFM-KFYSAhlFQNGSVLV 865
Cdd:pfam00069    3 VLRKLGSGSFGTVYKAK-----HRDTGKIVAIKKIKKEKIKKKKDKNILREIkiLK-KLNHPNIvRLYDA--FEDKDNLY 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801   866 --------GEL---YSYGTLLDDEDdlsAGLALIDLGQSIDmklfpKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGV 934
Cdd:pfam00069   75 lvleyvegGSLfdlLSEKGAFSERE---AKFIMKQILEGLE-----SGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSL 146

                          170
                   ....*....|.
gi 519666801   935 AATVYCMLFGT 945
Cdd:pfam00069  147 GCILYELLTGK 157
 
Name Accession Description Interval E-value
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 786-1016 1.13e-153

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: 456.62  E-value: 1.13e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  786 LVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLV 865
Cdd:cd14028     1 SVYVDHLLGEGAFAQVYQATQLDLNDAKSNQKFVLKVQKPANPWEFYIGTQLMERLKPSMRHLFIKFYSAHLFQNGSVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  866 GELYSYGTLLD-----------------------------------------------------------DEDDLSAGLA 886
Cdd:cd14028    81 GELYNYGTLLNainlykklpekvmpqplviyfamrilymveqlhdceiihgdikpdnfilgerflenddcEEDDLSHGLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  887 LIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLP 966
Cdd:cd14028   161 LIDLGQSIDMKLFPKGTAFTAKCETSGFQCTEMLSNKPWNYQTDYFGVAATVYCMLFGTYMKVKNEGGVWKPEGSFRRLP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 519666801  967 HLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRL 1016
Cdd:cd14028   241 HLELWNEFFHVMLNIPDCHSLPSLDALREKLKKVFQQHYTNKIRALRNRL 290
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
 786-1016 1.85e-92

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: 296.58  E-value: 1.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  786 LVYVHHLLGEGAFAQVYEATQGDLNdaKNKQKFVLKVQKPANPWEFYIGTQLMERL-KPSMQHMFMKFYSAHLFQNGSVL 864
Cdd:cd13981     1 TYVISKELGEGGYASVYLAKDDDEQ--SDGSLVALKVEKPPSIWEFYICDQLHSRLkNSRLRESISGAHSAHLFQDESIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  865 VGELYSYGTLLD-------------------------------------------------------------DEDDLSA 883
Cdd:cd13981    79 VMDYSSQGTLLDvvnkmknktgggmdeplamfftiellkvvealhevgiihgdikpdnfllrleicadwpgegENGWLSK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  884 GLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFR 963
Cdd:cd13981   159 GLKLIDFGRSIDMSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFGKYMELTQESGRWKINQNLK 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  964 RLPHLDMWNEFFHVMLNI-PDCHHLPSLDLLRQKLKK---VFQQHYTNK---IRALRNRL 1016
Cdd:cd13981   239 RYWQRDIWNKFFDTLLNPePSCNTLPLLEELRKILEEmeaWFEASLCNNlvvLRKLREIL 298
Mad3_BUB1_I smart00777
Mad3/BUB1 hoMad3/BUB1 homology region 1; Proteins containing this domain are checkpoint ...
 5-125 1.37e-48

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: 168.17  E-value: 1.37e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801      5 ENVLQMLEAHMQ-SYKGNDPLGEWERYIQWVEENFPEN--KEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSD 81
Cdd:smart00777    1 EQQRQAFEAELQdLYEGDDPLDLWLRYIKWTEENYPQGgkESGLLTLLERCIRYFEDDERYKNDPRYLKIWLKYAEYCDE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 519666801     82 LHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRG 125
Cdd:smart00777   81 PRELFQFLYSKGIGTKLALFYEEWAQLLEAAGRYKKADEVYQLG 124
Mad3_BUB1_I pfam08311
Mad3/BUB1 homology region 1; Proteins containing this domain are checkpoint proteins involved ...
 6-126 9.60e-46

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: 160.00  E-value: 9.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801     6 NVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPEN--KEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLH 83
Cdd:pfam08311    1 QERQQFEEEIREYDGDDPLEPWLRYIKWTEESYPQGgkESGLLELLERCTRYFKDDERYKNDPRYLKLWLKYADFCDDPR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 519666801    84 QFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGI 126
Cdd:pfam08311   81 DIFQFLYSNGIGTKLALFYEEWAELLERQGRFKEADEIYQLGI 123
STKc_BubR1_vert cd14029
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
 811-1016 3.94e-13

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: 71.44  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  811 DAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGS---------------------------V 863
Cdd:cd14029    40 DMEEAKAFAIKVDSQPVPWDFYITLQLKERLNDDFDTFFSEQTNCFLYQNGCislhkdinrftlqdilldseeiikeviV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  864 LV------------------GELYSYGTLLDDE-------DDLSAGLALIDLGQSIDMKLFPkgTIFTakceTSGFQCVE 918
Cdd:cd14029   120 LVtynllslveklhkaeivhGDLRPETLLLDDRifdpsssNELEGALKIVDFSHSMDLRLQP--TVSS----LRGFPIAQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  919 ------MLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDL 992
Cdd:cd14029   194 sesgqqFLAPQSSPYQVDLLGIADLAHLMLFREHLQVNQENSVWKISQNVSRLRGGNLWNKFFTKILNAAEGPTVCVLRE 273

                         250       260
                  ....*....|....*....|....*...
gi 519666801  993 LRQKLKKV----FQQHYTNKIRALRNRL 1016
Cdd:cd14029   274 LKGEMMELfdsgFQDKLCNYLIQLGMRL 301
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 793-941 5.47e-11

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: 63.44  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  793 LGEGAFAQVYEATqgdlnDAKNKQKFVLKVQKPANPWEFYIGTQL-MERLKpSMQH-MFMKFYSAHLFQNGSVLVGELYS 870
Cdd:cd00180     1 LGKGSFGKVYKAR-----DKETGKKVAVKVIPKEKLKKLLEELLReIEILK-KLNHpNIVKLYDVFETENFLYLVMEYCE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  871 YGTLLD---------DED-------DLSAGLA--------------------------LIDLGQSIDMKLFPKGTIFTAK 908
Cdd:cd00180    75 GGSLKDllkenkgplSEEealsilrQLLSALEylhsngiihrdlkpenilldsdgtvkLADFGLAKDLDSDDSLLKTTGG 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 519666801  909 CETSGFQCVEMLSNKPWNYQIDYFGVAATVYCM 941
Cdd:cd00180   155 TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 789-944 1.68e-05

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 47.52  E-value: 1.68e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801    789 VHHLLGEGAFAQVYEATqgdlnDAKNKQKFVLKVQKPANPWEFYIGT----QLMERLKpsmqHMF-MKFYSAHLFQNGSV 863
Cdd:smart00220    3 ILEKLGEGSFGKVYLAR-----DKKTGKLVAIKVIKKKKIKKDRERIlreiKILKKLK----HPNiVRLYDVFEDEDKLY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801    864 LVGELYSYGTLLD--------DEDD-------LSAGLA--------------------------LIDLGQSidmKLFPKG 902
Cdd:smart00220   74 LVMEYCEGGDLFDllkkrgrlSEDEarfylrqILSALEylhskgivhrdlkpenilldedghvkLADFGLA---RQLDPG 150

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 519666801    903 TIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFG 944
Cdd:smart00220  151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTG 192
Pkinase pfam00069
Protein kinase domain;
789-945 4.15e-04

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 43.00  E-value: 4.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801   789 VHHLLGEGAFAQVYEATqgdlnDAKNKQKFVLKVQKPANPWEFYIGTQLMER--LKpSMQHMFM-KFYSAhlFQNGSVLV 865
Cdd:pfam00069    3 VLRKLGSGSFGTVYKAK-----HRDTGKIVAIKKIKKEKIKKKKDKNILREIkiLK-KLNHPNIvRLYDA--FEDKDNLY 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801   866 --------GEL---YSYGTLLDDEDdlsAGLALIDLGQSIDmklfpKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGV 934
Cdd:pfam00069   75 lvleyvegGSLfdlLSEKGAFSERE---AKFIMKQILEGLE-----SGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSL 146

                          170
                   ....*....|.
gi 519666801   935 AATVYCMLFGT 945
Cdd:pfam00069  147 GCILYELLTGK 157
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 852-942 5.14e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 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: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 40.25  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666801  852 FYSA-------HLFQNgSVLVGELYSYGTLLDDEDDLSaglaLIDLGQSIDMKLFPKGTIFTAKceTSGFQCVEMLSNKP 924
Cdd:cd05608   109 FYTAqiisgleHLHQR-RIIYRDLKPENVLLDDDGNVR----ISDLGLAVELKDGQTKTKGYAG--TPGFMAPELLLGEE 181

                          90
                  ....*....|....*...
gi 519666801  925 WNYQIDYFGVAATVYCML 942
Cdd:cd05608   182 YDYSVDYFTLGVTLYEMI 199
 
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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