Kinesin light chain [Caenorhabditis elegans]
Protein Classification
tetratricopeptide repeat protein( domain architecture ID 12138572)
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 | |||||
| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
203-448 | 3.93e-30 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; : Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 118.19 E-value: 3.93e-30
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| Abraxas-like_domain super family | cl49623 | Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, ... |
29-133 | 7.76e-03 | |||||
Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, and similar domains found in insects and plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. BRCA1-A complex subunit Abraxas 1, also known as ABRA1, FAM175A, and CCDC98, is involved in DNA damage response and double-strand break (DSB) repair and acts as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex consists of Abraxas-1, BRCC36, BRE, MERIT40, and RAP80. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BRCA1-A opposes homologous recombination (HR) by suppressing resection. It has been shown for BIR (break-induced replication), an HR-subtype that involves extensive DNA resection and mutagenic DNA synthesis, that Abraxas inhibits DNA end resection through regulating the levels of SLX4/MUS81 chromatin loading at DSBs in response to Topoisomerase I (TOP1) inhibitor-induced DNA damage. Familial mutations in the BRCA1-A proteins Abraxas-1 and RAP80 predispose carriers to early-onset breast cancer, analogous to mutations in BRCA1 and BRCA2. BRCA1-A requires the tandem ubiquitin (UIM2)- and SUMO-interacting motifs (SIM) in RAP80 and the BRCC36 DUB to function in DNA repair. BRCA1-A recruits BRCA1 by binding its BRCT domains upon phosphorylation of a motif near the C-terminus of Abraxas-1. BRCA1 binding to BRCA1-A sequesters the HR activator BRCA1 about 2-10 kb distal from DNA break sites, which is posited to limit HR. It is currently unclear how BRCA1-A is functionalized and targeted by RAP80 and Abraxas-1, and how BRCA1 is inhibited when bound to the complex. BRISC complex subunit Abraxas 2 is also known as ABRO1, FAM175B or KIAA0157. The BRISC complex consists of BRCC36, MERIT40, BRE, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates; In the BRISC complex, Abraxas 2 binds SHMT2a, a metabolic enzyme enabling cancer growth in hypoxic environments, which prevents the BRCC36 from binding and cleaving ubiquitin chains. BRCC36 is the DUB for both BRCA1-A and BRISC. BRCC36 associates with pseudo-DUB proteins (Abraxas 1 in BRCA1-A, Abraxas 2 in BRISC), which lack the essential Zn2+-coordinating residues required for DUB catalytic function. BRCC36 in BRCA1-A and BRISC is activated by assembly due to interaction between Glu30 of BRCC36 and Asn170 in Abraxas 1 and Asn164 in Abraxas 2, respectively, which structures the activation loop and positions the catalytic Glu33, For the BRISC complex it has been shown that higher-order association of BRCC36 and Abraxas2 into a dimer of heterodimers (superdimer) is required for BRCC36 DUB activity. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade K63-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-KIAA0157 complexes have been found in Arabidopsis. The actual alignment was detected with superfamily member cd23519: Pssm-ID: 483963 Cd Length: 257 Bit Score: 38.41 E-value: 7.76e-03
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| Name | Accession | Description | Interval | E-value | |||||
| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
203-448 | 3.93e-30 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 118.19 E-value: 3.93e-30
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
219-484 | 6.07e-23 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 103.07 E-value: 6.07e-23
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
203-407 | 4.60e-22 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 100.38 E-value: 4.60e-22
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
205-485 | 9.78e-22 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 99.22 E-value: 9.78e-22
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
203-427 | 3.00e-18 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 88.44 E-value: 3.00e-18
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
289-364 | 1.34e-17 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 77.43 E-value: 1.34e-17
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
230-497 | 1.01e-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: 51.62 E-value: 1.01e-06
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| Mgr3-like | cd24145 | Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ... |
259-415 | 7.46e-05 | |||||
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; Mgr3 (also called mitochondrial genome-required protein 3) is a component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. The supercomplex is composed of Mgr1, Mgr3, and Yme1. Mgr3, together with Mgr1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Pssm-ID: 467945 [Multi-domain] Cd Length: 307 Bit Score: 45.03 E-value: 7.46e-05
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
332-364 | 1.75e-04 | |||||
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: 38.97 E-value: 1.75e-04
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| Abraxas-like_domain | cd23519 | Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, ... |
29-133 | 7.76e-03 | |||||
Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, and similar domains found in insects and plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. BRCA1-A complex subunit Abraxas 1, also known as ABRA1, FAM175A, and CCDC98, is involved in DNA damage response and double-strand break (DSB) repair and acts as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex consists of Abraxas-1, BRCC36, BRE, MERIT40, and RAP80. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BRCA1-A opposes homologous recombination (HR) by suppressing resection. It has been shown for BIR (break-induced replication), an HR-subtype that involves extensive DNA resection and mutagenic DNA synthesis, that Abraxas inhibits DNA end resection through regulating the levels of SLX4/MUS81 chromatin loading at DSBs in response to Topoisomerase I (TOP1) inhibitor-induced DNA damage. Familial mutations in the BRCA1-A proteins Abraxas-1 and RAP80 predispose carriers to early-onset breast cancer, analogous to mutations in BRCA1 and BRCA2. BRCA1-A requires the tandem ubiquitin (UIM2)- and SUMO-interacting motifs (SIM) in RAP80 and the BRCC36 DUB to function in DNA repair. BRCA1-A recruits BRCA1 by binding its BRCT domains upon phosphorylation of a motif near the C-terminus of Abraxas-1. BRCA1 binding to BRCA1-A sequesters the HR activator BRCA1 about 2-10 kb distal from DNA break sites, which is posited to limit HR. It is currently unclear how BRCA1-A is functionalized and targeted by RAP80 and Abraxas-1, and how BRCA1 is inhibited when bound to the complex. BRISC complex subunit Abraxas 2 is also known as ABRO1, FAM175B or KIAA0157. The BRISC complex consists of BRCC36, MERIT40, BRE, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates; In the BRISC complex, Abraxas 2 binds SHMT2a, a metabolic enzyme enabling cancer growth in hypoxic environments, which prevents the BRCC36 from binding and cleaving ubiquitin chains. BRCC36 is the DUB for both BRCA1-A and BRISC. BRCC36 associates with pseudo-DUB proteins (Abraxas 1 in BRCA1-A, Abraxas 2 in BRISC), which lack the essential Zn2+-coordinating residues required for DUB catalytic function. BRCC36 in BRCA1-A and BRISC is activated by assembly due to interaction between Glu30 of BRCC36 and Asn170 in Abraxas 1 and Asn164 in Abraxas 2, respectively, which structures the activation loop and positions the catalytic Glu33, For the BRISC complex it has been shown that higher-order association of BRCC36 and Abraxas2 into a dimer of heterodimers (superdimer) is required for BRCC36 DUB activity. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade K63-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-KIAA0157 complexes have been found in Arabidopsis. Pssm-ID: 467802 Cd Length: 257 Bit Score: 38.41 E-value: 7.76e-03
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| PRK13922 | PRK13922 | rod shape-determining protein MreC; Provisional |
92-143 | 8.82e-03 | |||||
rod shape-determining protein MreC; Provisional Pssm-ID: 237560 Cd Length: 276 Bit Score: 38.42 E-value: 8.82e-03
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| Name | Accession | Description | Interval | E-value | |||||
| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
203-448 | 3.93e-30 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 118.19 E-value: 3.93e-30
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
219-484 | 6.07e-23 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 103.07 E-value: 6.07e-23
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
203-407 | 4.60e-22 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 100.38 E-value: 4.60e-22
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
205-485 | 9.78e-22 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 99.22 E-value: 9.78e-22
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
189-400 | 4.49e-21 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 96.99 E-value: 4.49e-21
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
284-493 | 1.26e-20 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 91.22 E-value: 1.26e-20
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
203-427 | 3.00e-18 | |||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 88.44 E-value: 3.00e-18
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
289-364 | 1.34e-17 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 77.43 E-value: 1.34e-17
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
203-406 | 1.07e-16 | |||||
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: 80.54 E-value: 1.07e-16
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
216-478 | 2.42e-16 | |||||
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: 79.39 E-value: 2.42e-16
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
253-478 | 4.71e-16 | |||||
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: 78.62 E-value: 4.71e-16
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
330-404 | 7.16e-16 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 72.42 E-value: 7.16e-16
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
215-492 | 2.42e-15 | |||||
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: 76.31 E-value: 2.42e-15
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
246-322 | 2.91e-15 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 70.88 E-value: 2.91e-15
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
205-280 | 1.03e-14 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 69.34 E-value: 1.03e-14
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
254-406 | 1.76e-13 | |||||
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: 67.52 E-value: 1.76e-13
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
189-401 | 2.49e-13 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 69.56 E-value: 2.49e-13
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
204-362 | 3.08e-13 | |||||
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: 67.14 E-value: 3.08e-13
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
250-494 | 5.18e-13 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 71.56 E-value: 5.18e-13
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| TPR_10 | pfam13374 | Tetratricopeptide repeat; |
289-330 | 2.93e-12 | |||||
Tetratricopeptide repeat; Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 60.98 E-value: 2.93e-12
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
299-401 | 2.43e-11 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 60.18 E-value: 2.43e-11
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
242-404 | 3.19e-11 | |||||
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: 61.51 E-value: 3.19e-11
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
257-361 | 1.73e-10 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 57.87 E-value: 1.73e-10
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
288-404 | 1.87e-10 | |||||
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: 59.05 E-value: 1.87e-10
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
203-361 | 4.31e-10 | |||||
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: 58.43 E-value: 4.31e-10
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
203-362 | 3.44e-09 | |||||
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: 57.82 E-value: 3.44e-09
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
284-404 | 4.69e-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: 54.63 E-value: 4.69e-09
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
216-324 | 9.49e-09 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 52.87 E-value: 9.49e-09
|
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
231-383 | 1.06e-08 | |||||
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: 53.86 E-value: 1.06e-08
|
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| TPR_10 | pfam13374 | Tetratricopeptide repeat; |
247-287 | 2.44e-08 | |||||
Tetratricopeptide repeat; Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 49.81 E-value: 2.44e-08
|
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
288-493 | 3.91e-08 | |||||
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: 54.74 E-value: 3.91e-08
|
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
193-319 | 8.91e-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: 51.88 E-value: 8.91e-08
|
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| TPR_10 | pfam13374 | Tetratricopeptide repeat; |
331-372 | 1.75e-07 | |||||
Tetratricopeptide repeat; Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 47.50 E-value: 1.75e-07
|
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| CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
302-403 | 2.88e-07 | |||||
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 49.22 E-value: 2.88e-07
|
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| TPR_10 | pfam13374 | Tetratricopeptide repeat; |
206-246 | 7.98e-07 | |||||
Tetratricopeptide repeat; Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 45.57 E-value: 7.98e-07
|
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
230-497 | 1.01e-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: 51.62 E-value: 1.01e-06
|
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
373-488 | 1.13e-06 | |||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 46.23 E-value: 1.13e-06
|
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
192-360 | 1.25e-06 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 49.53 E-value: 1.25e-06
|
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
243-402 | 1.31e-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: 1.31e-06
|
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
251-401 | 1.00e-05 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.83 E-value: 1.00e-05
|
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| TPR_1 | pfam00515 | Tetratricopeptide repeat; |
332-364 | 1.06e-05 | |||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 42.41 E-value: 1.06e-05
|
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
203-319 | 1.43e-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: 44.80 E-value: 1.43e-05
|
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| TPR_10 | pfam13374 | Tetratricopeptide repeat; |
373-410 | 2.70e-05 | |||||
Tetratricopeptide repeat; Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 41.33 E-value: 2.70e-05
|
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
328-406 | 4.07e-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: 43.46 E-value: 4.07e-05
|
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| Mgr3-like | cd24145 | Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ... |
259-415 | 7.46e-05 | |||||
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; Mgr3 (also called mitochondrial genome-required protein 3) is a component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. The supercomplex is composed of Mgr1, Mgr3, and Yme1. Mgr3, together with Mgr1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Pssm-ID: 467945 [Multi-domain] Cd Length: 307 Bit Score: 45.03 E-value: 7.46e-05
|
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
203-319 | 1.12e-04 | |||||
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: 1.12e-04
|
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
332-364 | 1.75e-04 | |||||
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: 38.97 E-value: 1.75e-04
|
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| TPR_MalT | pfam17874 | MalT-like TPR region; This entry contains a series of TPR repeats. |
215-408 | 2.14e-04 | |||||
MalT-like TPR region; This entry contains a series of TPR repeats. Pssm-ID: 436107 [Multi-domain] Cd Length: 336 Bit Score: 43.45 E-value: 2.14e-04
|
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| CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
258-383 | 2.37e-04 | |||||
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 40.75 E-value: 2.37e-04
|
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| TPR_16 | pfam13432 | Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
254-319 | 5.41e-04 | |||||
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions. Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 38.47 E-value: 5.41e-04
|
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| TPR_7 | pfam13176 | Tetratricopeptide repeat; |
335-369 | 5.49e-04 | |||||
Tetratricopeptide repeat; Pssm-ID: 433012 [Multi-domain] Cd Length: 36 Bit Score: 37.52 E-value: 5.49e-04
|
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
203-277 | 5.94e-04 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 39.00 E-value: 5.94e-04
|
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| TPR_16 | pfam13432 | Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
216-275 | 6.58e-04 | |||||
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions. Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 38.09 E-value: 6.58e-04
|
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| TPR_16 | pfam13432 | Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
337-404 | 9.66e-04 | |||||
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions. Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 37.70 E-value: 9.66e-04
|
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
332-489 | 1.00e-03 | |||||
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: 39.40 E-value: 1.00e-03
|
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| 3a0801s09 | TIGR00990 | mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
245-361 | 1.17e-03 | |||||
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines] Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 41.51 E-value: 1.17e-03
|
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
230-404 | 1.31e-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: 41.61 E-value: 1.31e-03
|
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| TPR_2 | pfam07719 | Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
332-363 | 1.44e-03 | |||||
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: 36.35 E-value: 1.44e-03
|
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| TPR_16 | pfam13432 | Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
295-371 | 1.74e-03 | |||||
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions. Pssm-ID: 433202 [Multi-domain] Cd Length: 68 Bit Score: 36.93 E-value: 1.74e-03
|
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| TPR_1 | pfam00515 | Tetratricopeptide repeat; |
290-322 | 2.27e-03 | |||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 35.86 E-value: 2.27e-03
|
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
230-489 | 6.07e-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: 6.07e-03
|
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
290-322 | 6.66e-03 | |||||
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: 34.34 E-value: 6.66e-03
|
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| Abraxas-like_domain | cd23519 | Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, ... |
29-133 | 7.76e-03 | |||||
Abraxas-like domain of BRCA1-A complex subunit Abraxas 1, BRISC complex subunit Abraxas 2, and similar domains found in insects and plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. BRCA1-A complex subunit Abraxas 1, also known as ABRA1, FAM175A, and CCDC98, is involved in DNA damage response and double-strand break (DSB) repair and acts as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex consists of Abraxas-1, BRCC36, BRE, MERIT40, and RAP80. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BRCA1-A opposes homologous recombination (HR) by suppressing resection. It has been shown for BIR (break-induced replication), an HR-subtype that involves extensive DNA resection and mutagenic DNA synthesis, that Abraxas inhibits DNA end resection through regulating the levels of SLX4/MUS81 chromatin loading at DSBs in response to Topoisomerase I (TOP1) inhibitor-induced DNA damage. Familial mutations in the BRCA1-A proteins Abraxas-1 and RAP80 predispose carriers to early-onset breast cancer, analogous to mutations in BRCA1 and BRCA2. BRCA1-A requires the tandem ubiquitin (UIM2)- and SUMO-interacting motifs (SIM) in RAP80 and the BRCC36 DUB to function in DNA repair. BRCA1-A recruits BRCA1 by binding its BRCT domains upon phosphorylation of a motif near the C-terminus of Abraxas-1. BRCA1 binding to BRCA1-A sequesters the HR activator BRCA1 about 2-10 kb distal from DNA break sites, which is posited to limit HR. It is currently unclear how BRCA1-A is functionalized and targeted by RAP80 and Abraxas-1, and how BRCA1 is inhibited when bound to the complex. BRISC complex subunit Abraxas 2 is also known as ABRO1, FAM175B or KIAA0157. The BRISC complex consists of BRCC36, MERIT40, BRE, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates; In the BRISC complex, Abraxas 2 binds SHMT2a, a metabolic enzyme enabling cancer growth in hypoxic environments, which prevents the BRCC36 from binding and cleaving ubiquitin chains. BRCC36 is the DUB for both BRCA1-A and BRISC. BRCC36 associates with pseudo-DUB proteins (Abraxas 1 in BRCA1-A, Abraxas 2 in BRISC), which lack the essential Zn2+-coordinating residues required for DUB catalytic function. BRCC36 in BRCA1-A and BRISC is activated by assembly due to interaction between Glu30 of BRCC36 and Asn170 in Abraxas 1 and Asn164 in Abraxas 2, respectively, which structures the activation loop and positions the catalytic Glu33, For the BRISC complex it has been shown that higher-order association of BRCC36 and Abraxas2 into a dimer of heterodimers (superdimer) is required for BRCC36 DUB activity. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade K63-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-KIAA0157 complexes have been found in Arabidopsis. Pssm-ID: 467802 Cd Length: 257 Bit Score: 38.41 E-value: 7.76e-03
|
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| PRK13922 | PRK13922 | rod shape-determining protein MreC; Provisional |
92-143 | 8.82e-03 | |||||
rod shape-determining protein MreC; Provisional Pssm-ID: 237560 Cd Length: 276 Bit Score: 38.42 E-value: 8.82e-03
|
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| Blast search parameters | ||||
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