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peptidyl-prolyl cis-trans isomerase CYP40 isoform X2 [Oryza sativa Japonica Group]
CYP40/PPID family peptidylprolyl isomerase( domain architecture ID 11549474)
CYP40/PPID family cyclophilin-type peptidylprolyl isomerase contains tetratricopeptide (TPR) repeats and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins; similar to peptidyl-prolyl cis-trans isomerase D (PPID), or cyclophilin-40 (CYP40), that may also act as a co-chaperone in HSP90 complexes
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
cyclophilin_ABH_like | cd01926 | cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
26-193 | 3.87e-104 | ||||
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome. : Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 304.56 E-value: 3.87e-104
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
245-363 | 1.49e-09 | ||||
Tetratricopeptide (TPR) repeat [General function prediction only]; : Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.09 E-value: 1.49e-09
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Name | Accession | Description | Interval | E-value | ||||
cyclophilin_ABH_like | cd01926 | cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
26-193 | 3.87e-104 | ||||
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome. Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 304.56 E-value: 3.87e-104
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PTZ00060 | PTZ00060 | cyclophilin; Provisional |
24-195 | 2.53e-88 | ||||
cyclophilin; Provisional Pssm-ID: 240249 Cd Length: 183 Bit Score: 265.17 E-value: 2.53e-88
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Pro_isomerase | pfam00160 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
39-194 | 8.20e-60 | ||||
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function. Pssm-ID: 459694 [Multi-domain] Cd Length: 149 Bit Score: 190.54 E-value: 8.20e-60
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PpiB | COG0652 | Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
40-190 | 1.62e-57 | ||||
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 184.99 E-value: 1.62e-57
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
245-363 | 1.49e-09 | ||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.09 E-value: 1.49e-09
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TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
320-353 | 1.50e-05 | ||||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 41.66 E-value: 1.50e-05
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TPR_1 | pfam00515 | Tetratricopeptide repeat; |
320-353 | 2.03e-05 | ||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 41.25 E-value: 2.03e-05
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ACL4-like | cd24142 | Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
300-357 | 9.63e-05 | ||||
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present. Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 43.77 E-value: 9.63e-05
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PLN03088 | PLN03088 | SGT1, suppressor of G2 allele of SKP1; Provisional |
297-394 | 2.17e-03 | ||||
SGT1, suppressor of G2 allele of SKP1; Provisional Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 39.77 E-value: 2.17e-03
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
300-391 | 3.14e-03 | ||||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 39.68 E-value: 3.14e-03
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Name | Accession | Description | Interval | E-value | ||||
cyclophilin_ABH_like | cd01926 | cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
26-193 | 3.87e-104 | ||||
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome. Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 304.56 E-value: 3.87e-104
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PTZ00060 | PTZ00060 | cyclophilin; Provisional |
24-195 | 2.53e-88 | ||||
cyclophilin; Provisional Pssm-ID: 240249 Cd Length: 183 Bit Score: 265.17 E-value: 2.53e-88
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PLN03149 | PLN03149 | peptidyl-prolyl isomerase H (cyclophilin H); Provisional |
24-195 | 9.34e-74 | ||||
peptidyl-prolyl isomerase H (cyclophilin H); Provisional Pssm-ID: 178694 Cd Length: 186 Bit Score: 227.80 E-value: 9.34e-74
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cyclophilin | cd00317 | cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
29-191 | 2.00e-68 | ||||
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing. Pssm-ID: 238194 [Multi-domain] Cd Length: 146 Bit Score: 212.89 E-value: 2.00e-68
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Pro_isomerase | pfam00160 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
39-194 | 8.20e-60 | ||||
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function. Pssm-ID: 459694 [Multi-domain] Cd Length: 149 Bit Score: 190.54 E-value: 8.20e-60
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Cyclophilin_PPIL3_like | cd01928 | Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ... |
40-191 | 1.20e-57 | ||||
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known. Pssm-ID: 238909 [Multi-domain] Cd Length: 153 Bit Score: 185.33 E-value: 1.20e-57
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cyclophilin_WD40 | cd01927 | cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
40-191 | 1.30e-57 | ||||
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known. Pssm-ID: 238908 [Multi-domain] Cd Length: 148 Bit Score: 184.97 E-value: 1.30e-57
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PpiB | COG0652 | Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
40-190 | 1.62e-57 | ||||
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 184.99 E-value: 1.62e-57
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cyclophilin_RING | cd01923 | cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
40-191 | 1.30e-53 | ||||
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination. Pssm-ID: 238904 [Multi-domain] Cd Length: 159 Bit Score: 175.30 E-value: 1.30e-53
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cyclophilin_SpCYP2_like | cd01922 | cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ... |
40-190 | 4.53e-50 | ||||
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling. Pssm-ID: 238903 [Multi-domain] Cd Length: 146 Bit Score: 165.40 E-value: 4.53e-50
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cyclophilin_CeCYP16-like | cd01925 | cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ... |
40-201 | 1.62e-39 | ||||
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding. Pssm-ID: 238906 [Multi-domain] Cd Length: 171 Bit Score: 138.64 E-value: 1.62e-39
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PTZ00221 | PTZ00221 | cyclophilin; Provisional |
27-195 | 8.40e-36 | ||||
cyclophilin; Provisional Pssm-ID: 140248 Cd Length: 249 Bit Score: 131.53 E-value: 8.40e-36
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cyclophilin_RRM | cd01921 | cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ... |
39-189 | 2.15e-34 | ||||
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis. Pssm-ID: 238902 [Multi-domain] Cd Length: 166 Bit Score: 125.15 E-value: 2.15e-34
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cyclophilin_EcCYP_like | cd01920 | cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
40-189 | 3.39e-21 | ||||
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding. Pssm-ID: 238901 [Multi-domain] Cd Length: 155 Bit Score: 89.04 E-value: 3.39e-21
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cyclophilin_TLP40_like | cd01924 | cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
41-173 | 3.48e-13 | ||||
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation. Pssm-ID: 238905 Cd Length: 176 Bit Score: 67.47 E-value: 3.48e-13
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PRK10903 | PRK10903 | peptidylprolyl isomerase A; |
39-176 | 3.85e-13 | ||||
peptidylprolyl isomerase A; Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 67.56 E-value: 3.85e-13
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PRK10791 | PRK10791 | peptidylprolyl isomerase B; |
40-189 | 6.23e-11 | ||||
peptidylprolyl isomerase B; Pssm-ID: 182734 Cd Length: 164 Bit Score: 60.62 E-value: 6.23e-11
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
245-363 | 1.49e-09 | ||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.09 E-value: 1.49e-09
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
294-380 | 3.94e-08 | ||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 52.27 E-value: 3.94e-08
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
239-383 | 5.86e-08 | ||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 51.35 E-value: 5.86e-08
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
241-390 | 7.83e-08 | ||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 52.61 E-value: 7.83e-08
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
213-351 | 8.00e-08 | ||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 51.50 E-value: 8.00e-08
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
220-354 | 2.75e-07 | ||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 51.07 E-value: 2.75e-07
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
252-379 | 3.03e-07 | ||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 51.27 E-value: 3.03e-07
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
241-380 | 4.58e-07 | ||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 50.78 E-value: 4.58e-07
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
312-363 | 4.70e-07 | ||||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 48.46 E-value: 4.70e-07
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
289-363 | 8.87e-07 | ||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 49.62 E-value: 8.87e-07
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
297-379 | 2.91e-06 | ||||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 46.15 E-value: 2.91e-06
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
241-363 | 6.42e-06 | ||||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 45.38 E-value: 6.42e-06
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
297-377 | 8.19e-06 | ||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 44.01 E-value: 8.19e-06
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
232-379 | 8.48e-06 | ||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 47.03 E-value: 8.48e-06
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
241-375 | 9.14e-06 | ||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 47.68 E-value: 9.14e-06
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
245-352 | 1.04e-05 | ||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 43.62 E-value: 1.04e-05
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TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
320-353 | 1.50e-05 | ||||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 41.66 E-value: 1.50e-05
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TPR_1 | pfam00515 | Tetratricopeptide repeat; |
320-353 | 2.03e-05 | ||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 41.25 E-value: 2.03e-05
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TPR_8 | pfam13181 | Tetratricopeptide repeat; |
320-352 | 3.99e-05 | ||||
Tetratricopeptide repeat; Pssm-ID: 404131 [Multi-domain] Cd Length: 33 Bit Score: 40.07 E-value: 3.99e-05
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TPR_2 | pfam07719 | Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
320-351 | 5.69e-05 | ||||
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515. Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 39.81 E-value: 5.69e-05
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ACL4-like | cd24142 | Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
300-357 | 9.63e-05 | ||||
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present. Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 43.77 E-value: 9.63e-05
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
245-380 | 3.33e-04 | ||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.02 E-value: 3.33e-04
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
297-353 | 1.16e-03 | ||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 41.13 E-value: 1.16e-03
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PLN03088 | PLN03088 | SGT1, suppressor of G2 allele of SKP1; Provisional |
297-394 | 2.17e-03 | ||||
SGT1, suppressor of G2 allele of SKP1; Provisional Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 39.77 E-value: 2.17e-03
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TPR_19 | pfam14559 | Tetratricopeptide repeat; |
300-367 | 2.49e-03 | ||||
Tetratricopeptide repeat; Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.02 E-value: 2.49e-03
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
300-391 | 3.14e-03 | ||||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 39.68 E-value: 3.14e-03
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
297-396 | 4.47e-03 | ||||
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 39.30 E-value: 4.47e-03
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PLN03088 | PLN03088 | SGT1, suppressor of G2 allele of SKP1; Provisional |
303-352 | 6.60e-03 | ||||
SGT1, suppressor of G2 allele of SKP1; Provisional Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 38.23 E-value: 6.60e-03
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Blast search parameters | ||||
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