Os01g0977200 [Oryza sativa Japonica Group]
tetratricopeptide repeat protein( domain architecture ID 1000094)
tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
PRK10767 super family | cl35946 | chaperone protein DnaJ; Provisional |
322-390 | 8.07e-28 | |||||
chaperone protein DnaJ; Provisional The actual alignment was detected with superfamily member PRK10767: Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 113.70 E-value: 8.07e-28
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PEP_TPR_lipo super family | cl37187 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
24-301 | 3.04e-12 | |||||
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. The actual alignment was detected with superfamily member TIGR02917: Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 68.96 E-value: 3.04e-12
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Name | Accession | Description | Interval | E-value | |||||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
322-390 | 8.07e-28 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 113.70 E-value: 8.07e-28
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
326-390 | 5.65e-27 | |||||
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family. Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 110.77 E-value: 5.65e-27
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
326-389 | 1.11e-26 | |||||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 101.78 E-value: 1.11e-26
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
326-391 | 3.27e-24 | |||||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 97.47 E-value: 3.27e-24
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
325-384 | 5.04e-23 | |||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.53 E-value: 5.04e-23
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
326-381 | 2.10e-20 | |||||
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification. Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 84.13 E-value: 2.10e-20
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
322-390 | 9.00e-20 | |||||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 91.03 E-value: 9.00e-20
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
24-301 | 3.04e-12 | |||||
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: 68.96 E-value: 3.04e-12
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
59-332 | 1.05e-11 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 64.64 E-value: 1.05e-11
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PRK11189 | PRK11189 | lipoprotein NlpI; Provisional |
48-132 | 9.36e-04 | |||||
lipoprotein NlpI; Provisional Pssm-ID: 236875 [Multi-domain] Cd Length: 296 Bit Score: 41.03 E-value: 9.36e-04
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Name | Accession | Description | Interval | E-value | |||||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
322-390 | 8.07e-28 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 113.70 E-value: 8.07e-28
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
326-390 | 5.65e-27 | |||||
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family. Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 110.77 E-value: 5.65e-27
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
326-389 | 1.11e-26 | |||||
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 101.78 E-value: 1.11e-26
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
324-390 | 3.02e-24 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 103.73 E-value: 3.02e-24
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
326-391 | 3.27e-24 | |||||
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 97.47 E-value: 3.27e-24
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
321-390 | 3.68e-24 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 103.28 E-value: 3.68e-24
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
324-390 | 9.21e-24 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 102.18 E-value: 9.21e-24
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
321-390 | 3.47e-23 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 100.31 E-value: 3.47e-23
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
325-384 | 5.04e-23 | |||||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.53 E-value: 5.04e-23
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
321-390 | 1.08e-21 | |||||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 95.94 E-value: 1.08e-21
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
325-394 | 1.53e-21 | |||||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 95.69 E-value: 1.53e-21
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
324-390 | 3.44e-21 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 94.67 E-value: 3.44e-21
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
321-390 | 7.48e-21 | |||||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 93.74 E-value: 7.48e-21
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
325-395 | 1.44e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 92.69 E-value: 1.44e-20
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
326-381 | 2.10e-20 | |||||
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification. Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 84.13 E-value: 2.10e-20
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
325-390 | 2.30e-20 | |||||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 92.15 E-value: 2.30e-20
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
326-393 | 2.59e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 92.21 E-value: 2.59e-20
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
326-392 | 2.96e-20 | |||||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 91.98 E-value: 2.96e-20
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
325-393 | 3.99e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 91.65 E-value: 3.99e-20
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
321-390 | 4.97e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 91.42 E-value: 4.97e-20
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
322-390 | 8.63e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 90.21 E-value: 8.63e-20
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
322-390 | 9.00e-20 | |||||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 91.03 E-value: 9.00e-20
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
321-390 | 9.47e-20 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 90.63 E-value: 9.47e-20
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
322-391 | 1.05e-19 | |||||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 83.23 E-value: 1.05e-19
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
325-393 | 2.44e-19 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 89.30 E-value: 2.44e-19
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
325-389 | 1.33e-18 | |||||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 87.10 E-value: 1.33e-18
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
325-390 | 3.81e-18 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 84.61 E-value: 3.81e-18
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
326-390 | 6.12e-18 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 84.94 E-value: 6.12e-18
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
324-389 | 6.84e-18 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 84.82 E-value: 6.84e-18
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
325-389 | 1.68e-17 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 83.60 E-value: 1.68e-17
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
325-390 | 3.62e-16 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 79.65 E-value: 3.62e-16
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PRK10266 | PRK10266 | curved DNA-binding protein; |
325-390 | 2.16e-15 | |||||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 76.40 E-value: 2.16e-15
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
323-390 | 5.27e-15 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 76.14 E-value: 5.27e-15
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
325-393 | 7.29e-15 | |||||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 76.01 E-value: 7.29e-15
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
321-390 | 1.01e-14 | |||||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 75.43 E-value: 1.01e-14
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
24-301 | 3.04e-12 | |||||
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: 68.96 E-value: 3.04e-12
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
59-332 | 1.05e-11 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 64.64 E-value: 1.05e-11
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
327-390 | 3.06e-11 | |||||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 64.71 E-value: 3.06e-11
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
173-367 | 3.59e-11 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 65.01 E-value: 3.59e-11
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
46-320 | 4.97e-11 | |||||
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: 63.21 E-value: 4.97e-11
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
35-217 | 1.92e-10 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 62.70 E-value: 1.92e-10
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
174-396 | 1.96e-10 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 60.79 E-value: 1.96e-10
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
183-321 | 3.05e-10 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 62.32 E-value: 3.05e-10
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
326-382 | 1.90e-09 | |||||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 54.03 E-value: 1.90e-09
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
30-255 | 2.72e-09 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 57.32 E-value: 2.72e-09
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
174-315 | 3.01e-09 | |||||
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: 55.01 E-value: 3.01e-09
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
173-297 | 8.58e-09 | |||||
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: 54.04 E-value: 8.58e-09
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
33-214 | 1.17e-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: 53.66 E-value: 1.17e-08
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djlA | PRK09430 | co-chaperone DjlA; |
325-379 | 1.19e-08 | |||||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 55.97 E-value: 1.19e-08
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
24-124 | 7.26e-08 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 54.61 E-value: 7.26e-08
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
55-216 | 1.98e-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: 49.62 E-value: 1.98e-07
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PTZ00341 | PTZ00341 | Ring-infected erythrocyte surface antigen; Provisional |
327-390 | 7.56e-07 | |||||
Ring-infected erythrocyte surface antigen; Provisional Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 51.71 E-value: 7.56e-07
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
24-124 | 8.24e-07 | |||||
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: 48.26 E-value: 8.24e-07
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PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
29-302 | 1.11e-06 | |||||
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: 51.24 E-value: 1.11e-06
|
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
28-144 | 1.39e-06 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 50.76 E-value: 1.39e-06
|
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
179-352 | 2.59e-06 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 48.37 E-value: 2.59e-06
|
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
30-97 | 3.48e-06 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 47.99 E-value: 3.48e-06
|
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
63-255 | 1.07e-05 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.45 E-value: 1.07e-05
|
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
190-298 | 1.47e-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: 1.47e-05
|
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
43-124 | 2.28e-05 | |||||
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: 44.57 E-value: 2.28e-05
|
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
43-124 | 2.47e-05 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 42.85 E-value: 2.47e-05
|
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
24-126 | 4.72e-05 | |||||
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: 45.11 E-value: 4.72e-05
|
|||||||||
NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
30-136 | 5.46e-05 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 44.14 E-value: 5.46e-05
|
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
24-97 | 6.26e-05 | |||||
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: 42.87 E-value: 6.26e-05
|
|||||||||
LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
185-324 | 7.34e-05 | |||||
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: 44.33 E-value: 7.34e-05
|
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
30-109 | 7.79e-05 | |||||
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: 42.30 E-value: 7.79e-05
|
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ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
323-389 | 7.88e-05 | |||||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 44.64 E-value: 7.88e-05
|
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
181-302 | 1.56e-04 | |||||
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: 41.72 E-value: 1.56e-04
|
|||||||||
LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
24-217 | 2.21e-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: 42.79 E-value: 2.21e-04
|
|||||||||
BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
174-260 | 2.79e-04 | |||||
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: 40.95 E-value: 2.79e-04
|
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
24-120 | 7.16e-04 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 41.15 E-value: 7.16e-04
|
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PRK11189 | PRK11189 | lipoprotein NlpI; Provisional |
48-132 | 9.36e-04 | |||||
lipoprotein NlpI; Provisional Pssm-ID: 236875 [Multi-domain] Cd Length: 296 Bit Score: 41.03 E-value: 9.36e-04
|
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NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
174-269 | 1.51e-03 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 39.90 E-value: 1.51e-03
|
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
320-356 | 3.48e-03 | |||||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 37.14 E-value: 3.48e-03
|
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NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
30-124 | 6.44e-03 | |||||
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: 36.91 E-value: 6.44e-03
|
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
30-97 | 6.50e-03 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 35.92 E-value: 6.50e-03
|
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PHA03102 | PHA03102 | Small T antigen; Reviewed |
329-396 | 8.18e-03 | |||||
Small T antigen; Reviewed Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 36.96 E-value: 8.18e-03
|
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Blast search parameters | ||||
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