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Conserved domains on  [gi|398366685|ref|NP_010821|]
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Kre28p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Kre28 super family cl25921
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
1-382 7.54e-62

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


The actual alignment was detected with superfamily member pfam17097:

Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 202.73  E-value: 7.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685    1 MDTgsASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVnplrndeSLDVEGKEVFVNPKI 80
Cdd:pfam17097   1 MDT--STINGYEAQLRELEEQTAHSSEQVLTEQDKRLLGALRELTQSVIQLIEENSLV-------TVSGDAANLLIDPSG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685   81 LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE 160
Cdd:pfam17097  72 IEVKIRQLDQLVELLKVTHLEQETLDNFLRYTISSTDLLQLESVSDPKYASLEDEVSQLEDDTLTVLNQEIDQIKGDILQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  161 TGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTnkeDKNMMGEKDTILNSSDSDDFVEETYTNW-------QKLLF 233
Cdd:pfam17097 152 VAQEIADKQDQVNELCLETSNELDECWELLNELERLR---DQRITVEEQTSNEKDTELDPVEETYEEWkslqeslQQLEH 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  234 LQKQNQRLTKELKEMHEVKNqiirkgeqsKKEDSGHLMANESELCQSINLLTKFWEKHFLlkgSKTTILNFEIFTQLGKV 313
Cdd:pfam17097 229 LKEELDQLQKQKDSLEKVDK---------SSINRTQNDEESIQNTVQLNLLIDMWKSKFI---IHEKISNLELYPRSRKF 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366685  314 QFEIKDmQYIIAISLSDlkRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTkvQIFEVMDDIISEL 382
Cdd:pfam17097 297 QFRVAN-RYTIIIQLDK--GSTISNIELFTKDDPSIIPNRELRKDVLNEYLGTS--NIYQVLNDIIHRL 360
 
Name Accession Description Interval E-value
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
1-382 7.54e-62

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 202.73  E-value: 7.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685    1 MDTgsASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVnplrndeSLDVEGKEVFVNPKI 80
Cdd:pfam17097   1 MDT--STINGYEAQLRELEEQTAHSSEQVLTEQDKRLLGALRELTQSVIQLIEENSLV-------TVSGDAANLLIDPSG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685   81 LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE 160
Cdd:pfam17097  72 IEVKIRQLDQLVELLKVTHLEQETLDNFLRYTISSTDLLQLESVSDPKYASLEDEVSQLEDDTLTVLNQEIDQIKGDILQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  161 TGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTnkeDKNMMGEKDTILNSSDSDDFVEETYTNW-------QKLLF 233
Cdd:pfam17097 152 VAQEIADKQDQVNELCLETSNELDECWELLNELERLR---DQRITVEEQTSNEKDTELDPVEETYEEWkslqeslQQLEH 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  234 LQKQNQRLTKELKEMHEVKNqiirkgeqsKKEDSGHLMANESELCQSINLLTKFWEKHFLlkgSKTTILNFEIFTQLGKV 313
Cdd:pfam17097 229 LKEELDQLQKQKDSLEKVDK---------SSINRTQNDEESIQNTVQLNLLIDMWKSKFI---IHEKISNLELYPRSRKF 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366685  314 QFEIKDmQYIIAISLSDlkRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTkvQIFEVMDDIISEL 382
Cdd:pfam17097 297 QFRVAN-RYTIIIQLDK--GSTISNIELFTKDDPSIIPNRELRKDVLNEYLGTS--NIYQVLNDIIHRL 360
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
131-277 6.95e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685 131 KLNERVNDLKEEISNVQEsKIEQIKAEIQETGHNFAERQDLINELYleatgdiencwdslNELKNL--TNKEDKNMMGEK 208
Cdd:COG3883   41 ALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERR--------------EELGERarALYRSGGSVSYL 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366685 209 DTILNSSDSDDFVeetyTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEdsghLMANESEL 277
Cdd:COG3883  106 DVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAEL 166
glyc_debranch TIGR01531
glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic ...
66-184 7.45e-03

glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273673 [Multi-domain]  Cd Length: 1464  Bit Score: 38.67  E-value: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685    66 SLDV-EGKEVFVNPKIlsaKIKEFNKLMELLKLTYLEQETLDYFF-------------------RFTLSSTKPLQLDSEK 125
Cdd:TIGR01531  247 GLDIaEWEHRGVPALI---EHEHLNAIMYGIKVHVLPKLKLWEFYqvdvqkavndfkahwtqesSYVTNNIKDQSSDIIQ 323
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685   126 DPQFVKLNERVN-DLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEATGDIE 184
Cdd:TIGR01531  324 DPEYRRFGVTVNfETALRIFNRHNGDLKLEEDRGEKCSSSLATALNILNENLRLYRYDID 383
 
Name Accession Description Interval E-value
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
1-382 7.54e-62

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 202.73  E-value: 7.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685    1 MDTgsASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVnplrndeSLDVEGKEVFVNPKI 80
Cdd:pfam17097   1 MDT--STINGYEAQLRELEEQTAHSSEQVLTEQDKRLLGALRELTQSVIQLIEENSLV-------TVSGDAANLLIDPSG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685   81 LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE 160
Cdd:pfam17097  72 IEVKIRQLDQLVELLKVTHLEQETLDNFLRYTISSTDLLQLESVSDPKYASLEDEVSQLEDDTLTVLNQEIDQIKGDILQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  161 TGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTnkeDKNMMGEKDTILNSSDSDDFVEETYTNW-------QKLLF 233
Cdd:pfam17097 152 VAQEIADKQDQVNELCLETSNELDECWELLNELERLR---DQRITVEEQTSNEKDTELDPVEETYEEWkslqeslQQLEH 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685  234 LQKQNQRLTKELKEMHEVKNqiirkgeqsKKEDSGHLMANESELCQSINLLTKFWEKHFLlkgSKTTILNFEIFTQLGKV 313
Cdd:pfam17097 229 LKEELDQLQKQKDSLEKVDK---------SSINRTQNDEESIQNTVQLNLLIDMWKSKFI---IHEKISNLELYPRSRKF 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366685  314 QFEIKDmQYIIAISLSDlkRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTkvQIFEVMDDIISEL 382
Cdd:pfam17097 297 QFRVAN-RYTIIIQLDK--GSTISNIELFTKDDPSIIPNRELRKDVLNEYLGTS--NIYQVLNDIIHRL 360
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
131-277 6.95e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685 131 KLNERVNDLKEEISNVQEsKIEQIKAEIQETGHNFAERQDLINELYleatgdiencwdslNELKNL--TNKEDKNMMGEK 208
Cdd:COG3883   41 ALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERR--------------EELGERarALYRSGGSVSYL 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366685 209 DTILNSSDSDDFVeetyTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEdsghLMANESEL 277
Cdd:COG3883  106 DVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAEL 166
glyc_debranch TIGR01531
glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic ...
66-184 7.45e-03

glycogen debranching enzymye; glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273673 [Multi-domain]  Cd Length: 1464  Bit Score: 38.67  E-value: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685    66 SLDV-EGKEVFVNPKIlsaKIKEFNKLMELLKLTYLEQETLDYFF-------------------RFTLSSTKPLQLDSEK 125
Cdd:TIGR01531  247 GLDIaEWEHRGVPALI---EHEHLNAIMYGIKVHVLPKLKLWEFYqvdvqkavndfkahwtqesSYVTNNIKDQSSDIIQ 323
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366685   126 DPQFVKLNERVN-DLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEATGDIE 184
Cdd:TIGR01531  324 DPEYRRFGVTVNfETALRIFNRHNGDLKLEEDRGEKCSSSLATALNILNENLRLYRYDID 383
 
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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