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Conserved domains on  [gi|665393765|ref|NP_001287273|]
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uncharacterized protein Dmel_CG31278, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pep_deformylase super family cl00234
Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ...
 52-120 1.20e-18

Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents.


The actual alignment was detected with superfamily member cd00487:

Pssm-ID: 444773  Cd Length: 141  Bit Score: 76.37  E-value: 1.20e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665393765  52 TQIGDPVLRQQAALVPKehmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELP 120
Cdd:cd00487    2 VQYPDPVLRKKAKPVEE---FDDELKQLIDDMFETMYAAPGVGLAAPQIGVSKRIFVIDVPDEENKEPP 67
 
Name Accession Description Interval E-value
Pep_deformylase cd00487
Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ...
 52-120 1.20e-18

Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents.


Pssm-ID: 238271  Cd Length: 141  Bit Score: 76.37  E-value: 1.20e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665393765  52 TQIGDPVLRQQAALVPKehmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELP 120
Cdd:cd00487    2 VQYPDPVLRKKAKPVEE---FDDELKQLIDDMFETMYAAPGVGLAAPQIGVSKRIFVIDVPDEENKEPP 67
Pep_deformylase pfam01327
Polypeptide deformylase;
50-123 2.22e-18

Polypeptide deformylase;


Pssm-ID: 426202  Cd Length: 153  Bit Score: 76.08  E-value: 2.22e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393765   50 HFTQIGDPVLRQQAALVPKEhmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELPEAV 123
Cdd:pfam01327   2 PIVTYPDPVLRKKAEPVEEF--DDKELKKLIDDMLETMYAADGVGLAAPQVGVSKRIFVIDLPDGEEEPDPLVL 73
Def COG0242
Peptide deformylase [Translation, ribosomal structure and biogenesis];
53-123 6.18e-16

Peptide deformylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440012  Cd Length: 163  Bit Score: 70.12  E-value: 6.18e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665393765  53 QIGDPVLRQQAALVPKEhmaSPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELPEAV 123
Cdd:COG0242    8 QYGDPVLRKVAKPVTEF---DDELRALIDDMFETMYAAPGVGLAAPQVGVSLRLFVIDVSDEDGKGEPLVL 75
def PRK00150
peptide deformylase; Reviewed
 53-114 1.13e-11

peptide deformylase; Reviewed


Pssm-ID: 234668  Cd Length: 165  Bit Score: 58.98  E-value: 1.13e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665393765  53 QIGDPVLRQQAALVPKehmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGR 114
Cdd:PRK00150   8 RYGDPVLRKVAKPVEE---VDDELRKLIDDMFETMYAAPGVGLAAPQVGVSKRIIVIDVEDK 66
 
Name Accession Description Interval E-value
Pep_deformylase cd00487
Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ...
 52-120 1.20e-18

Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents.


Pssm-ID: 238271  Cd Length: 141  Bit Score: 76.37  E-value: 1.20e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665393765  52 TQIGDPVLRQQAALVPKehmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELP 120
Cdd:cd00487    2 VQYPDPVLRKKAKPVEE---FDDELKQLIDDMFETMYAAPGVGLAAPQIGVSKRIFVIDVPDEENKEPP 67
Pep_deformylase pfam01327
Polypeptide deformylase;
50-123 2.22e-18

Polypeptide deformylase;


Pssm-ID: 426202  Cd Length: 153  Bit Score: 76.08  E-value: 2.22e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393765   50 HFTQIGDPVLRQQAALVPKEhmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELPEAV 123
Cdd:pfam01327   2 PIVTYPDPVLRKKAEPVEEF--DDKELKKLIDDMLETMYAADGVGLAAPQVGVSKRIFVIDLPDGEEEPDPLVL 73
Def COG0242
Peptide deformylase [Translation, ribosomal structure and biogenesis];
53-123 6.18e-16

Peptide deformylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440012  Cd Length: 163  Bit Score: 70.12  E-value: 6.18e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665393765  53 QIGDPVLRQQAALVPKEhmaSPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGRIRKELPEAV 123
Cdd:COG0242    8 QYGDPVLRKVAKPVTEF---DDELRALIDDMFETMYAAPGVGLAAPQVGVSLRLFVIDVSDEDGKGEPLVL 75
def PRK00150
peptide deformylase; Reviewed
 53-114 1.13e-11

peptide deformylase; Reviewed


Pssm-ID: 234668  Cd Length: 165  Bit Score: 58.98  E-value: 1.13e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665393765  53 QIGDPVLRQQAALVPKehmASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEFKGR 114
Cdd:PRK00150   8 RYGDPVLRKVAKPVEE---VDDELRKLIDDMFETMYAAPGVGLAAPQVGVSKRIIVIDVEDK 66
PRK12846 PRK12846
peptide deformylase; Reviewed
 54-111 2.40e-10

peptide deformylase; Reviewed


Pssm-ID: 237227  Cd Length: 165  Bit Score: 55.20  E-value: 2.40e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665393765  54 IGDPVLRQQAALVpkEHMASPEIKAIVERMVKVLRKFDCVGIAAPQIGVSLRIIAMEF 111
Cdd:PRK12846   9 MPDPRLRRPAEPV--TAFDTEELQALIDDMFETMRAADGVGLAAPQIGVSLRVVVIDL 64
PRK09218 PRK09218
peptide deformylase; Validated
 57-108 8.82e-03

peptide deformylase; Validated


Pssm-ID: 181704  Cd Length: 136  Bit Score: 34.51  E-value: 8.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665393765  57 PVLRQQAALVPKEHMASPEIKAIVERMVKVLR--KFDCVGIAAPQIGVSLRIIA 108
Cdd:PRK09218   4 PIVKDQLFLSQKSQPATKEDLQLAQDLQDTLLanRDECVGMAANMIGVQKRIII 57
 
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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