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Conserved domains on  [gi|320543499|ref|NP_733375|]
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uncharacterized protein Dmel_CG31371, isoform B [Drosophila melanogaster]

Protein Classification

prolyl 4-hydroxylase subunit alpha( domain architecture ID 10551023)

prolyl 4-hydroxylase catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
30-158 1.40e-34

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


:

Pssm-ID: 462433  Cd Length: 135  Bit Score: 126.62  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543499   30 EQLQALLDTETQLIDGLRDYIERLERQLEEIRRETSAIEEIHSQVD-SVEEYMGNPLNVFGILKRFESVWPGLEQKANAT 108
Cdd:pfam08336   3 SGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADeDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMKTN 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320543499  109 LEMVFGERLS---DRQLTLPSEEDYEESLNHLLHLQSVYELDSNSLSLGVVNG 158
Cdd:pfam08336  83 QAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
30-158 1.40e-34

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 126.62  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543499   30 EQLQALLDTETQLIDGLRDYIERLERQLEEIRRETSAIEEIHSQVD-SVEEYMGNPLNVFGILKRFESVWPGLEQKANAT 108
Cdd:pfam08336   3 SGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADeDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMKTN 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320543499  109 LEMVFGERLS---DRQLTLPSEEDYEESLNHLLHLQSVYELDSNSLSLGVVNG 158
Cdd:pfam08336  83 QAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
30-158 1.40e-34

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 126.62  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543499   30 EQLQALLDTETQLIDGLRDYIERLERQLEEIRRETSAIEEIHSQVD-SVEEYMGNPLNVFGILKRFESVWPGLEQKANAT 108
Cdd:pfam08336   3 SGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADeDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMKTN 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 320543499  109 LEMVFGERLS---DRQLTLPSEEDYEESLNHLLHLQSVYELDSNSLSLGVVNG 158
Cdd:pfam08336  83 QAVGFLEQLTemrSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
 
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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