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Conserved domains on  [gi|6321363|ref|NP_011440|]
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Mps2p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPS2 super family cl26265
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
10-386 2.61e-48

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


The actual alignment was detected with superfamily member pfam17060:

Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 167.07  E-value: 2.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     10 FEYAWGQIDKPISGdFIYGKDLPKLIEIIENIFQKAQKSGSyelRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFN 89
Cdd:pfam17060   1 LDLVWLQVDRKRQG-FIYAKDFPSFITQCEEILKRGVNTNK---KLPLLSKTGMDLIDAFAKETEFFKIYKESFSEMFNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     90 LVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKflvenKNKNTEGAGISTPRK-------KLTESPIKLLSRNNIGKA 162
Cdd:pfam17060  77 LVGNNFKTVINKIFEDCDGIPASFISALELKEDVK-----SSPRSEADSLGTPIKvdllrnlKPQESPETPRRINRKYKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    163 LEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSdLQKARQVEDNQNSSRTSdpgsplvtgIDQKA 242
Cdd:pfam17060 152 LELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFE-FYKQHHEHGGNNSIKTA---------TKHEF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    243 ILEEFRRRLQRQTDTISFLKDQIRRERGlncsndkvshskRKHATTDGDGTFKNFISAvpsniwvkatIRIIVCFALLAG 322
Cdd:pfam17060 222 IISELKRKLQEQNRLIRILQEQIQFDPG------------ALHDNGPKNLVLNGAIAA----------VLPFLLFIFVIR 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321363    323 VLpyirKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLET-EYRSNANVDDAYSRVFG 386
Cdd:pfam17060 280 SL----IAVGGGKEDIGDATMALSWWERNNLLSRLAWFFRDVFDTDSaDFLEDEVVSDAYDKVFG 340
 
Name Accession Description Interval E-value
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
10-386 2.61e-48

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 167.07  E-value: 2.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     10 FEYAWGQIDKPISGdFIYGKDLPKLIEIIENIFQKAQKSGSyelRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFN 89
Cdd:pfam17060   1 LDLVWLQVDRKRQG-FIYAKDFPSFITQCEEILKRGVNTNK---KLPLLSKTGMDLIDAFAKETEFFKIYKESFSEMFNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     90 LVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKflvenKNKNTEGAGISTPRK-------KLTESPIKLLSRNNIGKA 162
Cdd:pfam17060  77 LVGNNFKTVINKIFEDCDGIPASFISALELKEDVK-----SSPRSEADSLGTPIKvdllrnlKPQESPETPRRINRKYKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    163 LEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSdLQKARQVEDNQNSSRTSdpgsplvtgIDQKA 242
Cdd:pfam17060 152 LELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFE-FYKQHHEHGGNNSIKTA---------TKHEF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    243 ILEEFRRRLQRQTDTISFLKDQIRRERGlncsndkvshskRKHATTDGDGTFKNFISAvpsniwvkatIRIIVCFALLAG 322
Cdd:pfam17060 222 IISELKRKLQEQNRLIRILQEQIQFDPG------------ALHDNGPKNLVLNGAIAA----------VLPFLLFIFVIR 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321363    323 VLpyirKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLET-EYRSNANVDDAYSRVFG 386
Cdd:pfam17060 280 SL----IAVGGGKEDIGDATMALSWWERNNLLSRLAWFFRDVFDTDSaDFLEDEVVSDAYDKVFG 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-265 4.34e-05

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: 45.82  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     152 KLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDL--QKARQVEDNQNSSRTSD 229
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqQKQILRERLANLERQLE 319
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 6321363     230 PGSplvtgidqkAILEEFRRRLQRQTDTISFLKDQI 265
Cdd:TIGR02168  320 ELE---------AQLEELESKLDELAEELAELEEKL 346
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-269 1.05e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363   152 KLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNssrtsdpG 231
Cdd:COG4913  679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-------L 751
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 6321363   232 SPLVTGIDQKAILEEFRRRLQRQTDTisfLKDQIRRER 269
Cdd:COG4913  752 EERFAAALGDAVERELRENLEERIDA---LRARLNRAE 786
 
Name Accession Description Interval E-value
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
10-386 2.61e-48

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 167.07  E-value: 2.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     10 FEYAWGQIDKPISGdFIYGKDLPKLIEIIENIFQKAQKSGSyelRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFN 89
Cdd:pfam17060   1 LDLVWLQVDRKRQG-FIYAKDFPSFITQCEEILKRGVNTNK---KLPLLSKTGMDLIDAFAKETEFFKIYKESFSEMFNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     90 LVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKflvenKNKNTEGAGISTPRK-------KLTESPIKLLSRNNIGKA 162
Cdd:pfam17060  77 LVGNNFKTVINKIFEDCDGIPASFISALELKEDVK-----SSPRSEADSLGTPIKvdllrnlKPQESPETPRRINRKYKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    163 LEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSdLQKARQVEDNQNSSRTSdpgsplvtgIDQKA 242
Cdd:pfam17060 152 LELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYDFLSREFE-FYKQHHEHGGNNSIKTA---------TKHEF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363    243 ILEEFRRRLQRQTDTISFLKDQIRRERGlncsndkvshskRKHATTDGDGTFKNFISAvpsniwvkatIRIIVCFALLAG 322
Cdd:pfam17060 222 IISELKRKLQEQNRLIRILQEQIQFDPG------------ALHDNGPKNLVLNGAIAA----------VLPFLLFIFVIR 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321363    323 VLpyirKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLET-EYRSNANVDDAYSRVFG 386
Cdd:pfam17060 280 SL----IAVGGGKEDIGDATMALSWWERNNLLSRLAWFFRDVFDTDSaDFLEDEVVSDAYDKVFG 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-265 4.34e-05

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: 45.82  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     152 KLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDL--QKARQVEDNQNSSRTSD 229
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqQKQILRERLANLERQLE 319
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 6321363     230 PGSplvtgidqkAILEEFRRRLQRQTDTISFLKDQI 265
Cdd:TIGR02168  320 ELE---------AQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
161-289 1.74e-04

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: 43.89  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363     161 KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKAR---QVEDNQNSSRTSDPGSPLVTG 237
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtelEAEIEELEERLEEAEEELAEA 780
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6321363     238 IDQKAILEE----FRRRLQRQTDTISFLKDQIR--RERGLNCSNDKVSHSKRKHATTD 289
Cdd:TIGR02168  781 EAEIEELEAqieqLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATER 838
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-269 1.05e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363   152 KLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNssrtsdpG 231
Cdd:COG4913  679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-------L 751
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 6321363   232 SPLVTGIDQKAILEEFRRRLQRQTDTisfLKDQIRRER 269
Cdd:COG4913  752 EERFAAALGDAVERELRENLEERIDA---LRARLNRAE 786
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
161-220 2.74e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363  161 KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVED 220
Cdd:COG1579  34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
142-267 3.16e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363   142 PRKKLTESPIklLSRNNIGK--ALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQekyASIQQRFSDL---QKAR 216
Cdd:COG4913  594 DRRRIRSRYV--LGFDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQERREALQ---RLAEYSWDEIdvaSAER 668
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6321363   217 QVEDNQNSSRTSDPGSPLVTGIDQ-----KAILEEFRRRLQRQTDTISFLKDQIRR 267
Cdd:COG4913  669 EIAELEAELERLDASSDDLAALEEqleelEAELEELEEELDELKGEIGRLEKELEQ 724
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
161-269 3.20e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321363  161 KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNssrtsdpgsplvtgIDQ 240
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--------------REL 314
                        90       100
                ....*....|....*....|....*....
gi 6321363  241 KAILEEFRRRLQRQTDTISFLKDQIRRER 269
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELE 343
 
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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