NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145332977|ref|NP_001078354|]
View 

temperature sensing protein-like protein [Arabidopsis thaliana]

Protein Classification

cell division cycle protein 123 family protein( domain architecture ID 371286)

cell division cycle protein 123 family protein similar to Acanthamoeba polyphaga mimivirus CDC123-like protein L884

Gene Ontology:  GO:0045948|GO:0007049|GO:1905143|GO:0051301

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
D123 super family cl23567
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
 14-199 4.35e-82

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.


The actual alignment was detected with superfamily member pfam07065:

Pssm-ID: 462079  Cd Length: 299  Bit Score: 246.30  E-value: 4.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   14 WYPRFKSLTIKTKFHKLPESFINYLIDDSgpFLLPHSVTNEDAMPNRVHNFEEEDDFQVPEEASDDEPLNRPSFPELEIE 93
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDG--IVLPDESDDSPAEDSESDDDNEYSDWEDDDDDDEEDAPPFPRFPELHAQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   94 IRESIETLGGTIIPKLNWSSPKDAAWISPSQNLSCTCFNEIALLFRSSDSLTHDLFNAYDSC--SDKVSSRPESFYLALR 171
Cdd:pfam07065  79 IKEAIEELGGAVFPKLNWSAPKDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCesEDSSPPEPIEYELVLR 158

                         170       180
                  ....*....|....*....|....*...
gi 145332977  172 KWYpSLKPEMEFRCFVKSNELVGICQRE 199
Cdd:pfam07065 159 KWF-DLNPALEFRCFVRDRKLIGISQRD 185
 
Name Accession Description Interval E-value
D123 pfam07065
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
 14-199 4.35e-82

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: 246.30  E-value: 4.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   14 WYPRFKSLTIKTKFHKLPESFINYLIDDSgpFLLPHSVTNEDAMPNRVHNFEEEDDFQVPEEASDDEPLNRPSFPELEIE 93
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDG--IVLPDESDDSPAEDSESDDDNEYSDWEDDDDDDEEDAPPFPRFPELHAQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   94 IRESIETLGGTIIPKLNWSSPKDAAWISPSQNLSCTCFNEIALLFRSSDSLTHDLFNAYDSC--SDKVSSRPESFYLALR 171
Cdd:pfam07065  79 IKEAIEELGGAVFPKLNWSAPKDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCesEDSSPPEPIEYELVLR 158

                         170       180
                  ....*....|....*....|....*...
gi 145332977  172 KWYpSLKPEMEFRCFVKSNELVGICQRE 199
Cdd:pfam07065 159 KWF-DLNPALEFRCFVRDRKLIGISQRD 185
 
Name Accession Description Interval E-value
D123 pfam07065
D123; This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known ...
 14-199 4.35e-82

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: 246.30  E-value: 4.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   14 WYPRFKSLTIKTKFHKLPESFINYLIDDSgpFLLPHSVTNEDAMPNRVHNFEEEDDFQVPEEASDDEPLNRPSFPELEIE 93
Cdd:pfam07065   1 WYPKFKKHTIKSRIIPLPPEFLDYLREDG--IVLPDESDDSPAEDSESDDDNEYSDWEDDDDDDEEDAPPFPRFPELHAQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332977   94 IRESIETLGGTIIPKLNWSSPKDAAWISPSQNLSCTCFNEIALLFRSSDSLTHDLFNAYDSC--SDKVSSRPESFYLALR 171
Cdd:pfam07065  79 IKEAIEELGGAVFPKLNWSAPKDAAWILPNNTLKCTSPNDVYLLLKSSDFIAHDLDHAFDDCesEDSSPPEPIEYELVLR 158

                         170       180
                  ....*....|....*....|....*...
gi 145332977  172 KWYpSLKPEMEFRCFVKSNELVGICQRE 199
Cdd:pfam07065 159 KWF-DLNPALEFRCFVRDRKLIGISQRD 185
 
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