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Conserved domains on  [gi|449464106|ref|XP_004149770|]
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uncharacterized protein LOC101208586 [Cucumis sativus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MMR_HSR1 super family cl47706
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
142-222 7.28e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


The actual alignment was detected with superfamily member pfam01926:

Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 36.06  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449464106  142 LIGPKGSGKSSLINRISKvfeedhfapERAQVScNSSGEdgTFFLHEYMILRKSKSFCLYDTRGLSNDPSDNIEMLKQWM 221
Cdd:pfam01926   4 LVGRPNVGKSTLINALTG---------AKAIVS-DYPGT--TRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFL 71

                  .
gi 449464106  222 S 222
Cdd:pfam01926  72 A 72
 
Name Accession Description Interval E-value
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
142-222 7.28e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 36.06  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449464106  142 LIGPKGSGKSSLINRISKvfeedhfapERAQVScNSSGEdgTFFLHEYMILRKSKSFCLYDTRGLSNDPSDNIEMLKQWM 221
Cdd:pfam01926   4 LVGRPNVGKSTLINALTG---------AKAIVS-DYPGT--TRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFL 71

                  .
gi 449464106  222 S 222
Cdd:pfam01926  72 A 72
 
Name Accession Description Interval E-value
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
142-222 7.28e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 36.06  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449464106  142 LIGPKGSGKSSLINRISKvfeedhfapERAQVScNSSGEdgTFFLHEYMILRKSKSFCLYDTRGLSNDPSDNIEMLKQWM 221
Cdd:pfam01926   4 LVGRPNVGKSTLINALTG---------AKAIVS-DYPGT--TRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFL 71

                  .
gi 449464106  222 S 222
Cdd:pfam01926  72 A 72
 
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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