hypothetical protein Th1_141 [Salmonella phage Th1]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| DUF1425 super family | cl12345 | Putative periplasmic lipoprotein; This bacterial family of proteins contains members described ... |
1-21 | 4.18e-03 | ||
Putative periplasmic lipoprotein; This bacterial family of proteins contains members described as putative lipoproteins, some are also known as YcfL. The function of this family is unknown. Family members have also been annotated as predicted periplasmic lipoproteins (COG5633), and appear to contain an N-terminal membrane lipoprotein lipid attachment side (pfam08139), which is not included in this alignment model. The actual alignment was detected with superfamily member COG5633: Pssm-ID: 472303 Cd Length: 128 Bit Score: 33.81 E-value: 4.18e-03
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| Name | Accession | Description | Interval | E-value | ||
| YcfL | COG5633 | Uncharacterized conserved protein YcfL [Function unknown]; |
1-21 | 4.18e-03 | ||
Uncharacterized conserved protein YcfL [Function unknown]; Pssm-ID: 444360 Cd Length: 128 Bit Score: 33.81 E-value: 4.18e-03
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| LPAM_1 | pfam08139 | Prokaryotic membrane lipoprotein lipid attachment site; In prokaryotes, membrane lipoproteins ... |
1-18 | 4.36e-03 | ||
Prokaryotic membrane lipoprotein lipid attachment site; In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached. Analysis of lipoprotein and non-lipoprotein signal peptides reveals that the two classes differ significantly only in the region close to the signal peptidase cleavage site. This region is apolar and has the consensus sequence LA(G,A) 1C in the lipoproteins, but is polar and has small, uncharged residues in positions - 3 and - 1 in the non-lipoproteins. specialized signal peptide containing a lipobox motif in the carboxyl region of the signal peptide carries a cysteine residue which is the invariable target for lipidation by lipoprotein diacylglyceryl transferase (Lgt). Lipidation at this residue serves to anchor the lipoprotein to the membrane. Lipidation has been considered to be a prerequisite for the action of lipoprotein signal peptidase (Lsp), which removes the signal peptide and leaves the cysteine of the lipobox as the new amino-terminal residue of the mature lipoprotein. Pssm-ID: 429834 Cd Length: 18 Bit Score: 31.51 E-value: 4.36e-03
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| Name | Accession | Description | Interval | E-value | ||
| YcfL | COG5633 | Uncharacterized conserved protein YcfL [Function unknown]; |
1-21 | 4.18e-03 | ||
Uncharacterized conserved protein YcfL [Function unknown]; Pssm-ID: 444360 Cd Length: 128 Bit Score: 33.81 E-value: 4.18e-03
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| LPAM_1 | pfam08139 | Prokaryotic membrane lipoprotein lipid attachment site; In prokaryotes, membrane lipoproteins ... |
1-18 | 4.36e-03 | ||
Prokaryotic membrane lipoprotein lipid attachment site; In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached. Analysis of lipoprotein and non-lipoprotein signal peptides reveals that the two classes differ significantly only in the region close to the signal peptidase cleavage site. This region is apolar and has the consensus sequence LA(G,A) 1C in the lipoproteins, but is polar and has small, uncharged residues in positions - 3 and - 1 in the non-lipoproteins. specialized signal peptide containing a lipobox motif in the carboxyl region of the signal peptide carries a cysteine residue which is the invariable target for lipidation by lipoprotein diacylglyceryl transferase (Lgt). Lipidation at this residue serves to anchor the lipoprotein to the membrane. Lipidation has been considered to be a prerequisite for the action of lipoprotein signal peptidase (Lsp), which removes the signal peptide and leaves the cysteine of the lipobox as the new amino-terminal residue of the mature lipoprotein. Pssm-ID: 429834 Cd Length: 18 Bit Score: 31.51 E-value: 4.36e-03
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| COG4259 | COG4259 | Uncharacterized conserved protein, DUF4810 domain [Function unknown]; |
1-23 | 6.45e-03 | ||
Uncharacterized conserved protein, DUF4810 domain [Function unknown]; Pssm-ID: 443401 [Multi-domain] Cd Length: 119 Bit Score: 33.02 E-value: 6.45e-03
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| Blast search parameters | ||||
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