M1 family metallopeptidase [Chloracidobacterium aggregatum]
Protein Classification
M1 family metallopeptidase( domain architecture ID 11416872)
M1 family metallopeptidase contains an active site with a catalytic zinc ion bound by two histidines and a glutamate present in an HEXXH motif; functions as an aminopeptidase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||
| PepN | COG0308 | Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; |
24-696 | 8.70e-63 | ||||||||||
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; : Pssm-ID: 440077 [Multi-domain] Cd Length: 609 Bit Score: 220.67 E-value: 8.70e-63
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| Name | Accession | Description | Interval | E-value | ||||||||||
| PepN | COG0308 | Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; |
24-696 | 8.70e-63 | ||||||||||
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; Pssm-ID: 440077 [Multi-domain] Cd Length: 609 Bit Score: 220.67 E-value: 8.70e-63
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| M1_APN_like | cd09603 | Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly ... |
36-512 | 1.14e-52 | ||||||||||
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established. Pssm-ID: 341066 [Multi-domain] Cd Length: 410 Bit Score: 187.79 E-value: 1.14e-52
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| Peptidase_M1 | pfam01433 | Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ... |
310-511 | 1.09e-17 | ||||||||||
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity. Pssm-ID: 426262 [Multi-domain] Cd Length: 219 Bit Score: 82.34 E-value: 1.09e-17
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
598-704 | 1.32e-09 | ||||||||||
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: 61.64 E-value: 1.32e-09
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
637-665 | 7.70e-06 | ||||||||||
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: 43.20 E-value: 7.70e-06
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| PRK02603 | PRK02603 | photosystem I assembly protein Ycf3; Provisional |
593-703 | 5.61e-05 | ||||||||||
photosystem I assembly protein Ycf3; Provisional Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 44.28 E-value: 5.61e-05
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| Name | Accession | Description | Interval | E-value | ||||||||||
| PepN | COG0308 | Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; |
24-696 | 8.70e-63 | ||||||||||
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism]; Pssm-ID: 440077 [Multi-domain] Cd Length: 609 Bit Score: 220.67 E-value: 8.70e-63
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| M1_APN_like | cd09603 | Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly ... |
36-512 | 1.14e-52 | ||||||||||
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established. Pssm-ID: 341066 [Multi-domain] Cd Length: 410 Bit Score: 187.79 E-value: 1.14e-52
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| M1_APN_like | cd09604 | Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains ... |
40-512 | 1.99e-39 | ||||||||||
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established. Pssm-ID: 341067 [Multi-domain] Cd Length: 440 Bit Score: 151.27 E-value: 1.99e-39
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| M1 | cd09595 | Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 ... |
40-492 | 5.61e-22 | ||||||||||
Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 hydrolase; The model represents the catalytic domains of M1 peptidase family members including aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile upon activation during catalysis. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells, making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown, while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals. Pssm-ID: 341058 [Multi-domain] Cd Length: 413 Bit Score: 99.06 E-value: 5.61e-22
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| M1_APN | cd09602 | Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the ... |
35-506 | 4.86e-19 | ||||||||||
Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the catalytic domain of bacterial and eukaryotic aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established. Pssm-ID: 341065 [Multi-domain] Cd Length: 440 Bit Score: 90.27 E-value: 4.86e-19
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| Peptidase_M1 | pfam01433 | Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ... |
310-511 | 1.09e-17 | ||||||||||
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity. Pssm-ID: 426262 [Multi-domain] Cd Length: 219 Bit Score: 82.34 E-value: 1.09e-17
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| M1_APN-Q_like | cd09601 | Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ... |
276-513 | 1.10e-17 | ||||||||||
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1); This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established. Pssm-ID: 341064 [Multi-domain] Cd Length: 442 Bit Score: 86.09 E-value: 1.10e-17
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
609-703 | 2.36e-14 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 73.50 E-value: 2.36e-14
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
608-703 | 9.42e-13 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 68.49 E-value: 9.42e-13
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
608-720 | 1.02e-12 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 68.49 E-value: 1.02e-12
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
602-704 | 5.77e-12 | ||||||||||
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: 63.67 E-value: 5.77e-12
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
593-725 | 1.01e-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: 66.29 E-value: 1.01e-11
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
608-726 | 1.67e-11 | ||||||||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 64.55 E-value: 1.67e-11
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
613-707 | 1.72e-11 | ||||||||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 60.95 E-value: 1.72e-11
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
609-704 | 3.13e-11 | ||||||||||
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: 61.75 E-value: 3.13e-11
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| CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
611-703 | 4.46e-11 | ||||||||||
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: 60.39 E-value: 4.46e-11
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
608-703 | 4.97e-11 | ||||||||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 66.17 E-value: 4.97e-11
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
582-703 | 3.39e-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: 59.20 E-value: 3.39e-10
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
630-703 | 8.06e-10 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 60.02 E-value: 8.06e-10
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| M1_like_TAF2 | cd09839 | TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ... |
292-512 | 1.18e-09 | ||||||||||
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues. Pssm-ID: 341074 [Multi-domain] Cd Length: 531 Bit Score: 61.48 E-value: 1.18e-09
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
598-704 | 1.32e-09 | ||||||||||
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: 61.64 E-value: 1.32e-09
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
613-704 | 1.50e-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: 56.66 E-value: 1.50e-08
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
621-703 | 1.72e-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: 53.47 E-value: 1.72e-08
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
617-707 | 2.07e-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: 56.28 E-value: 2.07e-08
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
609-703 | 2.30e-08 | ||||||||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 55.31 E-value: 2.30e-08
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
609-707 | 6.63e-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: 6.63e-08
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
598-704 | 1.53e-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: 53.58 E-value: 1.53e-07
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
617-720 | 1.95e-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: 50.39 E-value: 1.95e-07
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
640-707 | 2.32e-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: 52.81 E-value: 2.32e-07
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| TPR_1 | pfam00515 | Tetratricopeptide repeat; |
637-670 | 2.21e-06 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 44.72 E-value: 2.21e-06
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| HemYx | COG3071 | Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
611-707 | 2.87e-06 | ||||||||||
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown]; Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 49.91 E-value: 2.87e-06
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
609-720 | 3.12e-06 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 49.23 E-value: 3.12e-06
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
609-667 | 3.88e-06 | ||||||||||
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: 47.26 E-value: 3.88e-06
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
593-679 | 4.18e-06 | ||||||||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 49.99 E-value: 4.18e-06
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
637-665 | 7.70e-06 | ||||||||||
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: 43.20 E-value: 7.70e-06
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
592-665 | 1.39e-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: 45.00 E-value: 1.39e-05
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
638-704 | 3.59e-05 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 42.37 E-value: 3.59e-05
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| TPR_2 | pfam07719 | Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
639-664 | 5.15e-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: 40.58 E-value: 5.15e-05
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| PRK02603 | PRK02603 | photosystem I assembly protein Ycf3; Provisional |
593-703 | 5.61e-05 | ||||||||||
photosystem I assembly protein Ycf3; Provisional Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 44.28 E-value: 5.61e-05
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| TPR_12 | pfam13424 | Tetratricopeptide repeat; |
607-665 | 1.32e-04 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 40.83 E-value: 1.32e-04
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| PRK11447 | PRK11447 | cellulose synthase subunit BcsC; Provisional |
609-696 | 3.26e-04 | ||||||||||
cellulose synthase subunit BcsC; Provisional Pssm-ID: 183140 [Multi-domain] Cd Length: 1157 Bit Score: 44.30 E-value: 3.26e-04
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| TPR_16 | pfam13432 | Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ... |
613-667 | 4.00e-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: 39.24 E-value: 4.00e-04
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| TPR_17 | pfam13431 | Tetratricopeptide repeat; |
626-657 | 4.36e-04 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 433201 [Multi-domain] Cd Length: 34 Bit Score: 38.29 E-value: 4.36e-04
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| ycf3 | CHL00033 | photosystem I assembly protein Ycf3 |
616-700 | 8.58e-04 | ||||||||||
photosystem I assembly protein Ycf3 Pssm-ID: 176974 [Multi-domain] Cd Length: 168 Bit Score: 40.76 E-value: 8.58e-04
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| TPR_8 | pfam13181 | Tetratricopeptide repeat; |
639-665 | 1.25e-03 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 404131 [Multi-domain] Cd Length: 33 Bit Score: 36.61 E-value: 1.25e-03
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
613-667 | 1.77e-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: 1.77e-03
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| PRK11788 | PRK11788 | tetratricopeptide repeat protein; Provisional |
612-705 | 2.34e-03 | ||||||||||
tetratricopeptide repeat protein; Provisional Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 40.95 E-value: 2.34e-03
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
609-703 | 2.66e-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: 41.22 E-value: 2.66e-03
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| CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
608-665 | 3.10e-03 | ||||||||||
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: 38.05 E-value: 3.10e-03
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| YfgM | COG2976 | Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
612-707 | 5.48e-03 | ||||||||||
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms]; Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 38.68 E-value: 5.48e-03
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| PEP_TPR_lipo | TIGR02917 | putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
558-664 | 5.59e-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: 40.07 E-value: 5.59e-03
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
646-703 | 6.59e-03 | ||||||||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 36.69 E-value: 6.59e-03
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| TPR_11 | pfam13414 | TPR repeat; |
617-650 | 6.64e-03 | ||||||||||
TPR repeat; Pssm-ID: 315977 [Multi-domain] Cd Length: 42 Bit Score: 35.14 E-value: 6.64e-03
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| TPR_19 | pfam14559 | Tetratricopeptide repeat; |
616-665 | 8.44e-03 | ||||||||||
Tetratricopeptide repeat; Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 35.25 E-value: 8.44e-03
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| Blast search parameters | ||||
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