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Conserved domains on  [gi|530392538|ref|XP_005252695|]
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cell division cycle protein 123 homolog isoform X1 [Homo sapiens]

Protein Classification

cell division cycle protein 123( domain architecture ID 10537197)

cell division cycle protein 123 regulates the cell cycle in a nutrient dependent manner

PubMed:  15319434

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D123 pfam07065
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
14-282 6.23e-114

D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known as D123) proteins approximately 330 residues long. It has been shown that mutated variants of D123 exhibit temperature-dependent differences in their degradation rate. D123 proteins are regulators of eIF2, the central regulator of translational initiation. Family members include ATP-grasp enzymes belonging to the R2K clade, wherein one of the absolutely-conserved lysine residues has migrated to the RAGYNA domain which is a part of the core ATP-grasp module. This family is found in eukaryotes as well as NCDLVs and diverse bacteria. In eukaryotes, the domain is found in both the CDC123 enzymes and a related clade of proteins found in amoeboid organizms, while in bacteria it is observed embedded in polymorphic toxin loci.


:

Pssm-ID: 462079  Cd Length: 299  Bit Score: 331.05  E-value: 6.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   14 WYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEaEEIQWSDDENTATLT-------------- 79
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDGIVLPDESDDSPAEDSESDDDN-EYSDWEDDDDDDEEDappfprfpelhaqi 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   80 ---------------------DAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCT--DDSPDPCIEYELVLRK 136
Cdd:pfam07065  80 keaieelggavfpklnwsapkDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCEseDSSPPEPIEYELVLRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538  137 WCELIPGAEFRCFVKENKLIGISQRDYtQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRD-SRGKVWLIDF 215
Cdd:pfam07065 160 WFDLNPALEFRCFVRDRKLIGISQRDL-NYYDFLEELKDEIRDLIEEFFEEKIKPKFPDEDYVFDVYIPrPFDKVWLIDF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530392538  216 NPFGEVTDSLLFTWEELISEnnlngdfsEVDAQEQDSPAFRCTNSEVTVQ--PSPYLSYRLPKDFVDLS 282
Cdd:pfam07065 239 NPFAPRTDPLLFTWEELLEM--------DDTDEEEDDPEFRLVESEDNPRfaSKPYSANKVPKDVVDAS 299
 
Name Accession Description Interval E-value
D123 pfam07065
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
14-282 6.23e-114

D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known as D123) proteins approximately 330 residues long. It has been shown that mutated variants of D123 exhibit temperature-dependent differences in their degradation rate. D123 proteins are regulators of eIF2, the central regulator of translational initiation. Family members include ATP-grasp enzymes belonging to the R2K clade, wherein one of the absolutely-conserved lysine residues has migrated to the RAGYNA domain which is a part of the core ATP-grasp module. This family is found in eukaryotes as well as NCDLVs and diverse bacteria. In eukaryotes, the domain is found in both the CDC123 enzymes and a related clade of proteins found in amoeboid organizms, while in bacteria it is observed embedded in polymorphic toxin loci.


Pssm-ID: 462079  Cd Length: 299  Bit Score: 331.05  E-value: 6.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   14 WYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEaEEIQWSDDENTATLT-------------- 79
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDGIVLPDESDDSPAEDSESDDDN-EYSDWEDDDDDDEEDappfprfpelhaqi 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   80 ---------------------DAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCT--DDSPDPCIEYELVLRK 136
Cdd:pfam07065  80 keaieelggavfpklnwsapkDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCEseDSSPPEPIEYELVLRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538  137 WCELIPGAEFRCFVKENKLIGISQRDYtQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRD-SRGKVWLIDF 215
Cdd:pfam07065 160 WFDLNPALEFRCFVRDRKLIGISQRDL-NYYDFLEELKDEIRDLIEEFFEEKIKPKFPDEDYVFDVYIPrPFDKVWLIDF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530392538  216 NPFGEVTDSLLFTWEELISEnnlngdfsEVDAQEQDSPAFRCTNSEVTVQ--PSPYLSYRLPKDFVDLS 282
Cdd:pfam07065 239 NPFAPRTDPLLFTWEELLEM--------DDTDEEEDDPEFRLVESEDNPRfaSKPYSANKVPKDVVDAS 299
 
Name Accession Description Interval E-value
D123 pfam07065
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
14-282 6.23e-114

D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known as D123) proteins approximately 330 residues long. It has been shown that mutated variants of D123 exhibit temperature-dependent differences in their degradation rate. D123 proteins are regulators of eIF2, the central regulator of translational initiation. Family members include ATP-grasp enzymes belonging to the R2K clade, wherein one of the absolutely-conserved lysine residues has migrated to the RAGYNA domain which is a part of the core ATP-grasp module. This family is found in eukaryotes as well as NCDLVs and diverse bacteria. In eukaryotes, the domain is found in both the CDC123 enzymes and a related clade of proteins found in amoeboid organizms, while in bacteria it is observed embedded in polymorphic toxin loci.


Pssm-ID: 462079  Cd Length: 299  Bit Score: 331.05  E-value: 6.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   14 WYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEaEEIQWSDDENTATLT-------------- 79
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDGIVLPDESDDSPAEDSESDDDN-EYSDWEDDDDDDEEDappfprfpelhaqi 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538   80 ---------------------DAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCT--DDSPDPCIEYELVLRK 136
Cdd:pfam07065  80 keaieelggavfpklnwsapkDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCEseDSSPPEPIEYELVLRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392538  137 WCELIPGAEFRCFVKENKLIGISQRDYtQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRD-SRGKVWLIDF 215
Cdd:pfam07065 160 WFDLNPALEFRCFVRDRKLIGISQRDL-NYYDFLEELKDEIRDLIEEFFEEKIKPKFPDEDYVFDVYIPrPFDKVWLIDF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530392538  216 NPFGEVTDSLLFTWEELISEnnlngdfsEVDAQEQDSPAFRCTNSEVTVQ--PSPYLSYRLPKDFVDLS 282
Cdd:pfam07065 239 NPFAPRTDPLLFTWEELLEM--------DDTDEEEDDPEFRLVESEDNPRfaSKPYSANKVPKDVVDAS 299
 
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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