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conserved oligomeric Golgi complex subunit 8 isoform 4 [Homo sapiens]
Dor1 and Pep_deformylase domain-containing protein( domain architecture ID 10514062)
Dor1 and Pep_deformylase domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
Dor1 | pfam04124 | Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ... |
50-364 | 4.10e-160 | |||||
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35. : Pssm-ID: 427729 Cd Length: 315 Bit Score: 461.89 E-value: 4.10e-160
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Def super family | cl42281 | Peptide deformylase [Translation, ribosomal structure and biogenesis]; |
588-626 | 3.77e-13 | |||||
Peptide deformylase [Translation, ribosomal structure and biogenesis]; The actual alignment was detected with superfamily member COG0242: Pssm-ID: 440012 Cd Length: 163 Bit Score: 67.43 E-value: 3.77e-13
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Name | Accession | Description | Interval | E-value | |||||
Dor1 | pfam04124 | Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ... |
50-364 | 4.10e-160 | |||||
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35. Pssm-ID: 427729 Cd Length: 315 Bit Score: 461.89 E-value: 4.10e-160
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Def | COG0242 | Peptide deformylase [Translation, ribosomal structure and biogenesis]; |
588-626 | 3.77e-13 | |||||
Peptide deformylase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440012 Cd Length: 163 Bit Score: 67.43 E-value: 3.77e-13
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Pep_deformylase | pfam01327 | Polypeptide deformylase; |
588-626 | 7.85e-13 | |||||
Polypeptide deformylase; Pssm-ID: 426202 Cd Length: 153 Bit Score: 66.45 E-value: 7.85e-13
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def | PRK00150 | peptide deformylase; Reviewed |
588-626 | 3.42e-12 | |||||
peptide deformylase; Reviewed Pssm-ID: 234668 Cd Length: 165 Bit Score: 64.76 E-value: 3.42e-12
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Pep_deformylase | cd00487 | Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ... |
588-619 | 1.39e-11 | |||||
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: 62.50 E-value: 1.39e-11
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pept_deformyl | TIGR00079 | peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, ... |
588-635 | 9.19e-06 | |||||
peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, is a metalloenzyme that uses water to release formate from the N-terminal formyl-L-methionine of bacterial and chloroplast peptides. This enzyme should not be confused with formylmethionine deformylase (EC 3.5.1.31) which is active on free N-formyl methionine and has been reported from rat intestine. [Protein fate, Protein modification and repair] Pssm-ID: 272895 Cd Length: 161 Bit Score: 46.22 E-value: 9.19e-06
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Name | Accession | Description | Interval | E-value | |||||
Dor1 | pfam04124 | Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ... |
50-364 | 4.10e-160 | |||||
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35. Pssm-ID: 427729 Cd Length: 315 Bit Score: 461.89 E-value: 4.10e-160
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Def | COG0242 | Peptide deformylase [Translation, ribosomal structure and biogenesis]; |
588-626 | 3.77e-13 | |||||
Peptide deformylase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440012 Cd Length: 163 Bit Score: 67.43 E-value: 3.77e-13
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Pep_deformylase | pfam01327 | Polypeptide deformylase; |
588-626 | 7.85e-13 | |||||
Polypeptide deformylase; Pssm-ID: 426202 Cd Length: 153 Bit Score: 66.45 E-value: 7.85e-13
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def | PRK00150 | peptide deformylase; Reviewed |
588-626 | 3.42e-12 | |||||
peptide deformylase; Reviewed Pssm-ID: 234668 Cd Length: 165 Bit Score: 64.76 E-value: 3.42e-12
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Pep_deformylase | cd00487 | Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ... |
588-619 | 1.39e-11 | |||||
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: 62.50 E-value: 1.39e-11
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PRK12846 | PRK12846 | peptide deformylase; Reviewed |
588-622 | 1.58e-07 | |||||
peptide deformylase; Reviewed Pssm-ID: 237227 Cd Length: 165 Bit Score: 51.34 E-value: 1.58e-07
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pept_deformyl | TIGR00079 | peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, ... |
588-635 | 9.19e-06 | |||||
peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, is a metalloenzyme that uses water to release formate from the N-terminal formyl-L-methionine of bacterial and chloroplast peptides. This enzyme should not be confused with formylmethionine deformylase (EC 3.5.1.31) which is active on free N-formyl methionine and has been reported from rat intestine. [Protein fate, Protein modification and repair] Pssm-ID: 272895 Cd Length: 161 Bit Score: 46.22 E-value: 9.19e-06
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PRK09218 | PRK09218 | peptide deformylase; Validated |
588-618 | 7.48e-04 | |||||
peptide deformylase; Validated Pssm-ID: 181704 Cd Length: 136 Bit Score: 39.91 E-value: 7.48e-04
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Blast search parameters | ||||
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