NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6325000|ref|NP_015068|]
View 

Bbp1p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BBP1_N pfam15271
Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a ...
 10-170 1.39e-72

Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a spindle pole body component, interacts directly, though transiently, with the polo-box domain of Cdc5p. full length BBP1 localizes at the cytoplasmic side of the central plaque periphery of the spindle pole body (SPB) and plays an important role in inserting a duplication plaque into the nuclear envelope and assembling a functional inner plaque. Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge.


:

Pssm-ID: 373701  Cd Length: 151  Bit Score: 223.08  E-value: 1.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     10 GGIFGLFKWTKDALFGTDISPSMKYKDqeerrdrsrYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLP 89
Cdd:pfam15271   1 GGISGLFKWTMDALFGSKISPSRKYKE---------FAQDDTNYNMKGRNNERSSEQLRSRSNSWSGLDSSFYRKYDLLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     90 EYNENGFNsivNGDHHSKERIRSLRSPAPIVPREPLRN--EPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKL 167
Cdd:pfam15271  72 PSNEEDQD---NHDPRYRDRIESLMSPVHLHPRPPLNAndEPTDTFANKKFNNRRSGNSYSDSSIPFKSPQKDDPLISKL 148


                  ...
gi 6325000    168 FNK 170
Cdd:pfam15271 149 FGK 151
BBP1_C super family cl21125
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 218-383 3.46e-28

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


The actual alignment was detected with superfamily member pfam15272:

Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 109.02  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    218 EYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVL 297
Cdd:pfam15272   1 DYTSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSYKKKYLQTRNELINELKQSKKLYDNYYKLYSKYQQLKKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    298 DQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRnnERKDTSAG 377
Cdd:pfam15272  81 NESLDLQSTITNLESQLVDQAIDKDREIHNLNEKILSLELRNQELETKREIDKMKYESRIDELERQLKEQ--EYPNVSSS 158


                  ....*.
gi 6325000    378 SNIFST 383
Cdd:pfam15272 159 SPYFST 164
 
Name Accession Description Interval E-value
BBP1_N pfam15271
Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a ...
 10-170 1.39e-72

Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a spindle pole body component, interacts directly, though transiently, with the polo-box domain of Cdc5p. full length BBP1 localizes at the cytoplasmic side of the central plaque periphery of the spindle pole body (SPB) and plays an important role in inserting a duplication plaque into the nuclear envelope and assembling a functional inner plaque. Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge.


Pssm-ID: 373701  Cd Length: 151  Bit Score: 223.08  E-value: 1.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     10 GGIFGLFKWTKDALFGTDISPSMKYKDqeerrdrsrYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLP 89
Cdd:pfam15271   1 GGISGLFKWTMDALFGSKISPSRKYKE---------FAQDDTNYNMKGRNNERSSEQLRSRSNSWSGLDSSFYRKYDLLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     90 EYNENGFNsivNGDHHSKERIRSLRSPAPIVPREPLRN--EPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKL 167
Cdd:pfam15271  72 PSNEEDQD---NHDPRYRDRIESLMSPVHLHPRPPLNAndEPTDTFANKKFNNRRSGNSYSDSSIPFKSPQKDDPLISKL 148


                  ...
gi 6325000    168 FNK 170
Cdd:pfam15271 149 FGK 151
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 218-383 3.46e-28

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 109.02  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    218 EYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVL 297
Cdd:pfam15272   1 DYTSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSYKKKYLQTRNELINELKQSKKLYDNYYKLYSKYQQLKKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    298 DQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRnnERKDTSAG 377
Cdd:pfam15272  81 NESLDLQSTITNLESQLVDQAIDKDREIHNLNEKILSLELRNQELETKREIDKMKYESRIDELERQLKEQ--EYPNVSSS 158


                  ....*.
gi 6325000    378 SNIFST 383
Cdd:pfam15272 159 SPYFST 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-374 1.15e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     217 REYKKAYFDLfaqmdlnSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMR---------AELVNELK-KSKTLFENYYSL 286
Cdd:TIGR02168  284 EELQKELYAL-------ANEISRLEQQKQILRERLANLERQLEELEAQLEeleskldelAEELAELEeKLEELKEELESL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     287 GQKYKSLKKVLDQTISHEAELATSRER-------LYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNY-ESEIH 358
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELK 436

                          170
                   ....*....|....*.
gi 6325000     359 DLLLQLSLRNNERKDT 374
Cdd:TIGR02168  437 ELQAELEELEEELEEL 452
 
Name Accession Description Interval E-value
BBP1_N pfam15271
Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a ...
 10-170 1.39e-72

Spindle pole body component BBP1, Mps2-binding protein; This N-terminal domain of BBP1, a spindle pole body component, interacts directly, though transiently, with the polo-box domain of Cdc5p. full length BBP1 localizes at the cytoplasmic side of the central plaque periphery of the spindle pole body (SPB) and plays an important role in inserting a duplication plaque into the nuclear envelope and assembling a functional inner plaque. Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge.


Pssm-ID: 373701  Cd Length: 151  Bit Score: 223.08  E-value: 1.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     10 GGIFGLFKWTKDALFGTDISPSMKYKDqeerrdrsrYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLP 89
Cdd:pfam15271   1 GGISGLFKWTMDALFGSKISPSRKYKE---------FAQDDTNYNMKGRNNERSSEQLRSRSNSWSGLDSSFYRKYDLLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     90 EYNENGFNsivNGDHHSKERIRSLRSPAPIVPREPLRN--EPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKL 167
Cdd:pfam15271  72 PSNEEDQD---NHDPRYRDRIESLMSPVHLHPRPPLNAndEPTDTFANKKFNNRRSGNSYSDSSIPFKSPQKDDPLISKL 148


                  ...
gi 6325000    168 FNK 170
Cdd:pfam15271 149 FGK 151
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 218-383 3.46e-28

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 109.02  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    218 EYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVL 297
Cdd:pfam15272   1 DYTSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSYKKKYLQTRNELINELKQSKKLYDNYYKLYSKYQQLKKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    298 DQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRnnERKDTSAG 377
Cdd:pfam15272  81 NESLDLQSTITNLESQLVDQAIDKDREIHNLNEKILSLELRNQELETKREIDKMKYESRIDELERQLKEQ--EYPNVSSS 158


                  ....*.
gi 6325000    378 SNIFST 383
Cdd:pfam15272 159 SPYFST 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-374 1.15e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     217 REYKKAYFDLfaqmdlnSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMR---------AELVNELK-KSKTLFENYYSL 286
Cdd:TIGR02168  284 EELQKELYAL-------ANEISRLEQQKQILRERLANLERQLEELEAQLEeleskldelAEELAELEeKLEELKEELESL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000     287 GQKYKSLKKVLDQTISHEAELATSRER-------LYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNY-ESEIH 358
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELK 436

                          170
                   ....*....|....*.
gi 6325000     359 DLLLQLSLRNNERKDT 374
Cdd:TIGR02168  437 ELQAELEELEEELEEL 452
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 215-361 1.67e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.49  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325000    215 KNREYKKAYFDLFAQMDLNSRDLE-------DLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYySLG 287
Cdd:pfam05557  21 MELEHKRARIELEKKASALKRQLDresdrnqELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKE-SQL 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325000    288 QKYKSLKKVLDQTISheaELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIekdmQRDNYESEIHDLL 361
Cdd:pfam05557 100 ADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQ----LRQNLEKQQSSLA 166
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH