CheR family methyltransferase [Achromobacter aloeverae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CheR | COG1352 | Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
235-498 | 3.79e-106 | |||||
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; : Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 333.67 E-value: 3.79e-106
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| CheB-CheR_fusion | cd16434 | Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ... |
23-201 | 2.64e-89 | |||||
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors, fused with a CheR domain as well as other domains. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheB and cheR are typically found in the same operon. However, CheB and CheR are fused in multi-domain proteins in this subgroup. The CheR protein/domain includes an all-alpha N-terminal domain and an S-adenosylmethionine-dependent methyltransferase C-terminal domain. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. : Pssm-ID: 319753 Cd Length: 180 Bit Score: 284.65 E-value: 2.64e-89
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| PAS_10 | pfam13596 | PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS ... |
751-856 | 6.44e-28 | |||||
PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). : Pssm-ID: 404482 [Multi-domain] Cd Length: 106 Bit Score: 108.82 E-value: 6.44e-28
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| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
742-981 | 8.19e-23 | |||||
PAS domain [Signal transduction mechanisms]; : Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 99.33 E-value: 8.19e-23
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| ZapB | COG3074 | Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
669-749 | 7.22e-15 | |||||
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]; : Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 70.77 E-value: 7.22e-15
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| HisKA | pfam00512 | His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
998-1027 | 4.17e-05 | |||||
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases. : Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 42.58 E-value: 4.17e-05
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| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
549-647 | 7.68e-04 | |||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. : Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 39.92 E-value: 7.68e-04
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| Name | Accession | Description | Interval | E-value | |||||
| CheR | COG1352 | Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
235-498 | 3.79e-106 | |||||
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 333.67 E-value: 3.79e-106
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| MeTrc | smart00138 | Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
235-496 | 5.18e-90 | |||||
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues. Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 289.96 E-value: 5.18e-90
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| CheB-CheR_fusion | cd16434 | Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ... |
23-201 | 2.64e-89 | |||||
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors, fused with a CheR domain as well as other domains. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheB and cheR are typically found in the same operon. However, CheB and CheR are fused in multi-domain proteins in this subgroup. The CheR protein/domain includes an all-alpha N-terminal domain and an S-adenosylmethionine-dependent methyltransferase C-terminal domain. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. Pssm-ID: 319753 Cd Length: 180 Bit Score: 284.65 E-value: 2.64e-89
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| CheB | COG2201 | Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ... |
21-207 | 9.99e-66 | |||||
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains [Signal transduction mechanisms]; Pssm-ID: 441803 Cd Length: 193 Bit Score: 219.96 E-value: 9.99e-66
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| CheB_methylest | pfam01339 | CheB methylesterase; |
24-198 | 1.27e-65 | |||||
CheB methylesterase; Pssm-ID: 460166 Cd Length: 178 Bit Score: 219.22 E-value: 1.27e-65
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| CheR | pfam01739 | CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
300-489 | 4.49e-57 | |||||
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM. Pssm-ID: 426403 Cd Length: 190 Bit Score: 195.19 E-value: 4.49e-57
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| PRK10611 | PRK10611 | protein-glutamate O-methyltransferase CheR; |
232-476 | 3.08e-35 | |||||
protein-glutamate O-methyltransferase CheR; Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 136.02 E-value: 3.08e-35
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| PAS_10 | pfam13596 | PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS ... |
751-856 | 6.44e-28 | |||||
PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 404482 [Multi-domain] Cd Length: 106 Bit Score: 108.82 E-value: 6.44e-28
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| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
742-981 | 8.19e-23 | |||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 99.33 E-value: 8.19e-23
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| PRK12555 | PRK12555 | chemotaxis-specific protein-glutamate methyltransferase CheB; |
8-202 | 1.88e-22 | |||||
chemotaxis-specific protein-glutamate methyltransferase CheB; Pssm-ID: 237135 [Multi-domain] Cd Length: 337 Bit Score: 99.96 E-value: 1.88e-22
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| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
862-981 | 6.36e-16 | |||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 75.02 E-value: 6.36e-16
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| ZapB | COG3074 | Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
669-749 | 7.22e-15 | |||||
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 70.77 E-value: 7.22e-15
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| PAS_9 | pfam13426 | PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
883-975 | 7.57e-09 | |||||
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 54.00 E-value: 7.57e-09
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| PRK11360 | PRK11360 | two-component system sensor histidine kinase AtoS; |
865-1016 | 4.25e-08 | |||||
two-component system sensor histidine kinase AtoS; Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 57.29 E-value: 4.25e-08
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| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
872-974 | 5.30e-07 | |||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 49.17 E-value: 5.30e-07
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| CENP-F_leu_zip | pfam10473 | Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
670-755 | 5.91e-07 | |||||
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance. Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 49.99 E-value: 5.91e-07
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| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
717-870 | 1.02e-06 | |||||
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]; Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 52.66 E-value: 1.02e-06
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| PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
863-920 | 2.38e-06 | |||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 46.24 E-value: 2.38e-06
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| HisKA | pfam00512 | His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
998-1027 | 4.17e-05 | |||||
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases. Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 42.58 E-value: 4.17e-05
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-754 | 1.15e-04 | |||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.15e-04
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| HisKA | smart00388 | His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
998-1027 | 1.33e-04 | |||||
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases. Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 41.01 E-value: 1.33e-04
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| HisKA | cd00082 | Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
997-1025 | 1.34e-04 | |||||
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes. Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 41.04 E-value: 1.34e-04
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| KdpD | COG2205 | K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
997-1028 | 3.63e-04 | |||||
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 43.36 E-value: 3.63e-04
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| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
549-647 | 7.68e-04 | |||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 39.92 E-value: 7.68e-04
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
659-752 | 7.93e-04 | |||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.93e-04
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| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
754-865 | 2.84e-03 | |||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 38.81 E-value: 2.84e-03
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| Spc7 | smart00787 | Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
667-754 | 3.41e-03 | |||||
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association. Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.41e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| CheR | COG1352 | Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
235-498 | 3.79e-106 | ||||||
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 333.67 E-value: 3.79e-106
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| MeTrc | smart00138 | Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
235-496 | 5.18e-90 | ||||||
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues. Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 289.96 E-value: 5.18e-90
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| CheB-CheR_fusion | cd16434 | Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ... |
23-201 | 2.64e-89 | ||||||
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors, fused with a CheR domain as well as other domains. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheB and cheR are typically found in the same operon. However, CheB and CheR are fused in multi-domain proteins in this subgroup. The CheR protein/domain includes an all-alpha N-terminal domain and an S-adenosylmethionine-dependent methyltransferase C-terminal domain. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. Pssm-ID: 319753 Cd Length: 180 Bit Score: 284.65 E-value: 2.64e-89
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| CheB | COG2201 | Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ... |
21-207 | 9.99e-66 | ||||||
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains [Signal transduction mechanisms]; Pssm-ID: 441803 Cd Length: 193 Bit Score: 219.96 E-value: 9.99e-66
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| CheB_methylest | pfam01339 | CheB methylesterase; |
24-198 | 1.27e-65 | ||||||
CheB methylesterase; Pssm-ID: 460166 Cd Length: 178 Bit Score: 219.22 E-value: 1.27e-65
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| CheR | pfam01739 | CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
300-489 | 4.49e-57 | ||||||
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM. Pssm-ID: 426403 Cd Length: 190 Bit Score: 195.19 E-value: 4.49e-57
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| CheB | cd16433 | Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the ... |
23-201 | 1.11e-54 | ||||||
Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheR and cheB have a strong preference to occur in the same operon, and a subgroup contains multidomain proteins with CheB-CheR fusions. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. Pssm-ID: 319752 Cd Length: 181 Bit Score: 187.97 E-value: 1.11e-54
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| CheB_Rec | cd16432 | Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ... |
23-201 | 2.21e-37 | ||||||
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain with a REC domain at the N-terminus. CheB is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. The N-terminal regulatory (REC) domain blocks the active site of the C-terminal domain until it is phosphorylated. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. Pssm-ID: 319751 Cd Length: 184 Bit Score: 138.65 E-value: 2.21e-37
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| PRK10611 | PRK10611 | protein-glutamate O-methyltransferase CheR; |
232-476 | 3.08e-35 | ||||||
protein-glutamate O-methyltransferase CheR; Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 136.02 E-value: 3.08e-35
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| CheB_like | cd16351 | methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; ... |
23-201 | 1.22e-33 | ||||||
methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. CheB family members may also contain an N-terminal regulatory (REC) domain, which blocks the active site of the C-terminal domain until it is phosphorylated, or a CheR domain; typically cheB and cheR occur in the same operon. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR. Pssm-ID: 319750 Cd Length: 184 Bit Score: 128.07 E-value: 1.22e-33
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| PAS_10 | pfam13596 | PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS ... |
751-856 | 6.44e-28 | ||||||
PAS domain; This is a sensor domain that recognizes O2, CO and NO (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 404482 [Multi-domain] Cd Length: 106 Bit Score: 108.82 E-value: 6.44e-28
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| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
742-981 | 8.19e-23 | ||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 99.33 E-value: 8.19e-23
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| PRK12555 | PRK12555 | chemotaxis-specific protein-glutamate methyltransferase CheB; |
8-202 | 1.88e-22 | ||||||
chemotaxis-specific protein-glutamate methyltransferase CheB; Pssm-ID: 237135 [Multi-domain] Cd Length: 337 Bit Score: 99.96 E-value: 1.88e-22
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| PRK00742 | PRK00742 | chemotaxis-specific protein-glutamate methyltransferase CheB; |
6-198 | 1.63e-19 | ||||||
chemotaxis-specific protein-glutamate methyltransferase CheB; Pssm-ID: 234828 [Multi-domain] Cd Length: 354 Bit Score: 91.36 E-value: 1.63e-19
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| NtrB | COG3852 | Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
859-1025 | 5.33e-19 | ||||||
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 90.29 E-value: 5.33e-19
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| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
858-1095 | 5.69e-17 | ||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 81.99 E-value: 5.69e-17
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| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
862-981 | 6.36e-16 | ||||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 75.02 E-value: 6.36e-16
|
||||||||||
| KinE | COG5809 | Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
738-1018 | 4.87e-15 | ||||||
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 79.25 E-value: 4.87e-15
|
||||||||||
| ZapB | COG3074 | Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
669-749 | 7.22e-15 | ||||||
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 70.77 E-value: 7.22e-15
|
||||||||||
| CheR_N | pfam03705 | CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
234-285 | 1.55e-12 | ||||||
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase. Pssm-ID: 461017 [Multi-domain] Cd Length: 53 Bit Score: 63.22 E-value: 1.55e-12
|
||||||||||
| CwlO1 | COG3883 | Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
671-788 | 5.27e-11 | ||||||
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown]; Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 66.01 E-value: 5.27e-11
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
667-757 | 7.75e-11 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 65.31 E-value: 7.75e-11
|
||||||||||
| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
876-1025 | 6.74e-10 | ||||||
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]; Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 62.67 E-value: 6.74e-10
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
667-772 | 1.02e-09 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 1.02e-09
|
||||||||||
| PAS_9 | pfam13426 | PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
883-975 | 7.57e-09 | ||||||
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 54.00 E-value: 7.57e-09
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
664-756 | 7.75e-09 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 7.75e-09
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
666-756 | 9.41e-09 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 9.41e-09
|
||||||||||
| KinA | COG5805 | Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
715-1018 | 3.54e-08 | ||||||
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 57.43 E-value: 3.54e-08
|
||||||||||
| PRK11360 | PRK11360 | two-component system sensor histidine kinase AtoS; |
865-1016 | 4.25e-08 | ||||||
two-component system sensor histidine kinase AtoS; Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 57.29 E-value: 4.25e-08
|
||||||||||
| PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
863-974 | 2.15e-07 | ||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 50.49 E-value: 2.15e-07
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
669-757 | 2.48e-07 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 2.48e-07
|
||||||||||
| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
872-974 | 5.30e-07 | ||||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 49.17 E-value: 5.30e-07
|
||||||||||
| CENP-F_leu_zip | pfam10473 | Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
670-755 | 5.91e-07 | ||||||
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance. Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 49.99 E-value: 5.91e-07
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
667-754 | 6.92e-07 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 6.92e-07
|
||||||||||
| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
717-870 | 1.02e-06 | ||||||
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]; Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 52.66 E-value: 1.02e-06
|
||||||||||
| Golgin_A5 | pfam09787 | Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
665-758 | 1.35e-06 | ||||||
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1. Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 51.68 E-value: 1.35e-06
|
||||||||||
| HIP1_clath_bdg | pfam16515 | Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
665-743 | 2.27e-06 | ||||||
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding. Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 46.93 E-value: 2.27e-06
|
||||||||||
| PAS | smart00091 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
863-920 | 2.38e-06 | ||||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. Pssm-ID: 214512 Cd Length: 67 Bit Score: 46.24 E-value: 2.38e-06
|
||||||||||
| EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
667-776 | 2.48e-06 | ||||||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.48e-06
|
||||||||||
| PAS_4 | pfam08448 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
757-859 | 5.40e-06 | ||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 46.25 E-value: 5.40e-06
|
||||||||||
| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
669-751 | 7.08e-06 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 7.08e-06
|
||||||||||
| RocR | COG3829 | RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
859-999 | 1.53e-05 | ||||||
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms]; Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 49.00 E-value: 1.53e-05
|
||||||||||
| WalK | COG5002 | Sensor histidine kinase WalK [Signal transduction mechanisms]; |
813-1028 | 1.84e-05 | ||||||
Sensor histidine kinase WalK [Signal transduction mechanisms]; Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 48.40 E-value: 1.84e-05
|
||||||||||
| RocR | COG3829 | RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
739-871 | 1.90e-05 | ||||||
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms]; Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 48.61 E-value: 1.90e-05
|
||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
666-829 | 2.94e-05 | ||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.94e-05
|
||||||||||
| PAS | pfam00989 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
750-855 | 3.19e-05 | ||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 44.33 E-value: 3.19e-05
|
||||||||||
| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
735-865 | 3.42e-05 | ||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 46.94 E-value: 3.42e-05
|
||||||||||
| HisKA | pfam00512 | His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
998-1027 | 4.17e-05 | ||||||
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases. Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 42.58 E-value: 4.17e-05
|
||||||||||
| ZapB | pfam06005 | Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
666-733 | 4.70e-05 | ||||||
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation. Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 42.64 E-value: 4.70e-05
|
||||||||||
| HMMR_N | pfam15905 | Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
659-751 | 6.88e-05 | ||||||
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate. Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.34 E-value: 6.88e-05
|
||||||||||
| EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
664-757 | 1.05e-04 | ||||||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.05e-04
|
||||||||||
| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
884-1028 | 1.12e-04 | ||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 45.67 E-value: 1.12e-04
|
||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-754 | 1.15e-04 | ||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.15e-04
|
||||||||||
| Myosin_tail_1 | pfam01576 | Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
646-745 | 1.20e-04 | ||||||
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament. Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.20e-04
|
||||||||||
| HisKA | smart00388 | His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
998-1027 | 1.33e-04 | ||||||
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases. Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 41.01 E-value: 1.33e-04
|
||||||||||
| HisKA | cd00082 | Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
997-1025 | 1.34e-04 | ||||||
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes. Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 41.04 E-value: 1.34e-04
|
||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-756 | 1.88e-04 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.88e-04
|
||||||||||
| COG4251 | COG4251 | Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
750-1025 | 2.01e-04 | ||||||
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms]; Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 45.16 E-value: 2.01e-04
|
||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-754 | 3.21e-04 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.21e-04
|
||||||||||
| PRK13560 | PRK13560 | hypothetical protein; Provisional |
674-948 | 3.21e-04 | ||||||
hypothetical protein; Provisional Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 45.05 E-value: 3.21e-04
|
||||||||||
| KdpD | COG2205 | K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
997-1028 | 3.63e-04 | ||||||
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 43.36 E-value: 3.63e-04
|
||||||||||
| COG4026 | COG4026 | Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
667-743 | 4.68e-04 | ||||||
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only]; Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 43.56 E-value: 4.68e-04
|
||||||||||
| Mplasa_alph_rch | TIGR04523 | helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
667-755 | 5.12e-04 | ||||||
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown. Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 5.12e-04
|
||||||||||
| HCR | pfam07111 | Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
655-746 | 7.27e-04 | ||||||
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation. Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 7.27e-04
|
||||||||||
| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
549-647 | 7.68e-04 | ||||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 39.92 E-value: 7.68e-04
|
||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
659-752 | 7.93e-04 | ||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.93e-04
|
||||||||||
| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-759 | 8.22e-04 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 8.22e-04
|
||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
659-747 | 9.65e-04 | ||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.65e-04
|
||||||||||
| EnvC | COG4942 | Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
667-757 | 1.01e-03 | ||||||
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.01e-03
|
||||||||||
| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-756 | 1.04e-03 | ||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.04e-03
|
||||||||||
| CENP-K | pfam11802 | Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) ... |
667-752 | 1.11e-03 | ||||||
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) centromere components (the others being CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S) that are identified as assembling on the CENP-A nucleosome associated complex, NAC. The CENP-A NAC is essential, as disruption of the complex causes errors of chromosome alignment and segregation that preclude cell survival despite continued centromere-derived mitotic checkpoint signalling. CENP-K is centromere-associated through its interaction with one or more components of the CENP-A NAC. Pssm-ID: 463355 [Multi-domain] Cd Length: 263 Bit Score: 41.98 E-value: 1.11e-03
|
||||||||||
| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-764 | 1.13e-03 | ||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.13e-03
|
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| Mplasa_alph_rch | TIGR04523 | helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
667-751 | 1.16e-03 | ||||||
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown. Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 1.16e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
659-747 | 1.17e-03 | ||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.17e-03
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| Leu_zip | pfam15294 | Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
660-745 | 1.32e-03 | ||||||
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2). Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.00 E-value: 1.32e-03
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
667-759 | 1.33e-03 | ||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.33e-03
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| ZapB | COG3074 | Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
705-752 | 1.33e-03 | ||||||
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 38.80 E-value: 1.33e-03
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| Sec20 | pfam03908 | Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway. |
668-727 | 1.37e-03 | ||||||
Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway. Pssm-ID: 112708 Cd Length: 92 Bit Score: 38.94 E-value: 1.37e-03
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
664-753 | 1.49e-03 | ||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.49e-03
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| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
653-760 | 1.52e-03 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.52e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
666-756 | 1.58e-03 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.58e-03
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
667-749 | 1.70e-03 | ||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.70e-03
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| ClpA | COG0542 | ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
667-763 | 1.74e-03 | ||||||
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.74e-03
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| WEMBL | pfam05701 | Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
670-758 | 2.00e-03 | ||||||
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like". Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 2.00e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-754 | 2.20e-03 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.20e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
667-754 | 2.25e-03 | ||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.25e-03
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| DR0291 | COG1579 | Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-743 | 2.45e-03 | ||||||
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]; Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.45e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-761 | 2.71e-03 | ||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.71e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-756 | 2.83e-03 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.83e-03
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| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
754-865 | 2.84e-03 | ||||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 38.81 E-value: 2.84e-03
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| DR0291 | COG1579 | Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-761 | 2.85e-03 | ||||||
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]; Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.85e-03
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| Spc7 | smart00787 | Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
667-754 | 3.41e-03 | ||||||
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association. Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.41e-03
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| ATG16 | pfam08614 | Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
654-752 | 3.47e-03 | ||||||
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 3.47e-03
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| CwlO1 | COG3883 | Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
659-761 | 4.40e-03 | ||||||
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown]; Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.40e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-756 | 5.17e-03 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.17e-03
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| Uso1_p115_C | pfam04871 | Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
665-743 | 6.16e-03 | ||||||
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another. Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 37.76 E-value: 6.16e-03
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| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
667-751 | 6.87e-03 | ||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 6.87e-03
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| SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
330-475 | 7.31e-03 | ||||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 39.13 E-value: 7.31e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-756 | 8.17e-03 | ||||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.17e-03
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| Tar | COG0840 | Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
647-746 | 8.28e-03 | ||||||
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 40.00 E-value: 8.28e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
667-759 | 8.50e-03 | ||||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 8.50e-03
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
667-753 | 8.82e-03 | ||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.82e-03
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| PAS_4 | pfam08448 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
875-979 | 9.38e-03 | ||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 37.01 E-value: 9.38e-03
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| Blast search parameters | ||||
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