STAT5-HKRR [Load driver vector pLDBUF]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||
| STAT5_DBD | cd16849 | DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
332-489 | 9.06e-105 | ||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the DNA-binding domain (DBD) of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 4), which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The DNA binding domain has an Ig-like fold. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. : Pssm-ID: 341087 Cd Length: 159 Bit Score: 329.84 E-value: 9.06e-105
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| SH2_STAT5b | cd10420 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-717 | 7.12e-101 | ||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5b proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. : Pssm-ID: 198283 Cd Length: 145 Bit Score: 318.56 E-value: 7.12e-101
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| STAT5_CCD | cd16855 | Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
139-330 | 1.05e-88 | ||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. : Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 286.47 E-value: 1.05e-88
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| STAT_int | pfam02865 | STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ... |
2-124 | 5.73e-53 | ||||||||||
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017. : Pssm-ID: 460728 Cd Length: 119 Bit Score: 181.26 E-value: 5.73e-53
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| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
755-1187 | 1.03e-44 | ||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; : Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 165.47 E-value: 1.03e-44
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| PRK11107 super family | cl35992 | hybrid sensory histidine kinase BarA; Provisional |
827-1470 | 1.22e-43 | ||||||||||
hybrid sensory histidine kinase BarA; Provisional The actual alignment was detected with superfamily member PRK11107: Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 173.11 E-value: 1.22e-43
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| Name | Accession | Description | Interval | E-value | |||||||||||
| STAT5_DBD | cd16849 | DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
332-489 | 9.06e-105 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the DNA-binding domain (DBD) of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 4), which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The DNA binding domain has an Ig-like fold. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. Pssm-ID: 341087 Cd Length: 159 Bit Score: 329.84 E-value: 9.06e-105
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| SH2_STAT5b | cd10420 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-717 | 7.12e-101 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5b proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198283 Cd Length: 145 Bit Score: 318.56 E-value: 7.12e-101
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| STAT5_CCD | cd16855 | Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
139-330 | 1.05e-88 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 286.47 E-value: 1.05e-88
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| STAT_bind | pfam02864 | STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ... |
336-469 | 1.34e-63 | |||||||||||
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. This family represents the DNA binding domain of STAT, which has an ig-like fold. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460727 Cd Length: 132 Bit Score: 212.06 E-value: 1.34e-63
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| STAT_alpha | pfam01017 | STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ... |
145-324 | 1.80e-59 | |||||||||||
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460026 Cd Length: 167 Bit Score: 201.68 E-value: 1.80e-59
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| STAT_int | pfam02865 | STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ... |
2-124 | 5.73e-53 | |||||||||||
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460728 Cd Length: 119 Bit Score: 181.26 E-value: 5.73e-53
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| STAT_int | smart00964 | STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ... |
2-125 | 4.28e-49 | |||||||||||
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain. Pssm-ID: 214942 Cd Length: 120 Bit Score: 170.16 E-value: 4.28e-49
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| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
755-1187 | 1.03e-44 | |||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 165.47 E-value: 1.03e-44
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| PRK11107 | PRK11107 | hybrid sensory histidine kinase BarA; Provisional |
827-1470 | 1.22e-43 | |||||||||||
hybrid sensory histidine kinase BarA; Provisional Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 173.11 E-value: 1.22e-43
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| REC_hyHK_CKI1_RcsC-like | cd17546 | phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
1350-1466 | 1.81e-41 | |||||||||||
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 148.00 E-value: 1.81e-41
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| CheY | COG0784 | CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
1347-1475 | 2.26e-35 | |||||||||||
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms]; Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 131.13 E-value: 2.26e-35
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| HATPase_EvgS-ArcB-TorS-like | cd16922 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
1112-1186 | 6.79e-34 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 126.45 E-value: 6.79e-34
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| Response_reg | pfam00072 | Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
1350-1466 | 1.82e-31 | |||||||||||
Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain. Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 119.56 E-value: 1.82e-31
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| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
1113-1186 | 3.08e-27 | |||||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 107.35 E-value: 3.08e-27
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| TMAO_torS | TIGR02956 | TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
747-1479 | 1.53e-24 | |||||||||||
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems] Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 111.79 E-value: 1.53e-24
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| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
1113-1188 | 9.98e-23 | |||||||||||
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 94.36 E-value: 9.98e-23
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| PRK11466 | PRK11466 | hybrid sensory histidine kinase TorS; Provisional |
753-1186 | 1.30e-20 | |||||||||||
hybrid sensory histidine kinase TorS; Provisional Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 98.82 E-value: 1.30e-20
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| SH2 | pfam00017 | SH2 domain; |
589-668 | 4.29e-13 | |||||||||||
SH2 domain; Pssm-ID: 425423 [Multi-domain] Cd Length: 77 Bit Score: 65.70 E-value: 4.29e-13
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| REC | smart00448 | cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ... |
1349-1408 | 1.22e-11 | |||||||||||
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues. Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 61.05 E-value: 1.22e-11
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| SH2 | smart00252 | Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ... |
596-636 | 1.79e-10 | |||||||||||
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae. Pssm-ID: 214585 [Multi-domain] Cd Length: 84 Bit Score: 58.78 E-value: 1.79e-10
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
29-243 | 2.42e-04 | |||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.42e-04
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-303 | 1.22e-03 | |||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.22e-03
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| Name | Accession | Description | Interval | E-value | |||||||||||
| STAT5_DBD | cd16849 | DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
332-489 | 9.06e-105 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the DNA-binding domain (DBD) of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 4), which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The DNA binding domain has an Ig-like fold. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. Pssm-ID: 341087 Cd Length: 159 Bit Score: 329.84 E-value: 9.06e-105
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| SH2_STAT5b | cd10420 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-717 | 7.12e-101 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5b proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198283 Cd Length: 145 Bit Score: 318.56 E-value: 7.12e-101
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| SH2_STAT5 | cd10376 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 ... |
573-711 | 3.88e-94 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. Pssm-ID: 198239 Cd Length: 137 Bit Score: 299.20 E-value: 3.88e-94
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| STAT5_CCD | cd16855 | Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
139-330 | 1.05e-88 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency. Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 286.47 E-value: 1.05e-88
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| SH2_STAT5a | cd10421 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-717 | 1.74e-85 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5a proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198284 Cd Length: 140 Bit Score: 275.00 E-value: 1.74e-85
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| STAT_DBD | cd14801 | DNA-binding domain of Signal Transducer and Activator of Transcription (STAT); This family ... |
332-488 | 7.31e-73 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription (STAT); This family consists of the DNA binding domain (DBD) of the STAT proteins (Signal Transducer and Activator of Transcription, or Signal Transduction And Transcription), which are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. STAT proteins regulate several aspects of growth, survival and differentiation in cells. The transcription factors of this family are activated by JAK (Janus kinase) and dysregulation of this pathway is frequently observed in primary tumors and leads to immunosuppression, increased angiogenesis and enhanced survival of tumors. There are seven mammalian STAT family members that have been identified: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6. STAT proteins consist of six structural regions: N-terminal domain (ND)/protein interaction domain, coiled-coil domain (CCD)/STAT all alpha domain, DNA-binding domain (DBD), linker domain (LK), a Src homology 2 (SH2) domain, and C-terminal transcriptional activation domain (TA) that includes two conserved phosphorylation sites (tyrosine and serine residues). STAT1 and STAT3 have the greatest diversity of biological functions among the 7 known members of the STAT family. The DNA binding domain of STAT has an Ig-like fold. DNA binding specificity experiments of different STAT proteins show that STAT5A specificity is more similar to that of STAT6 than that of STAT1, as also seen from the evolutionary relationships. Pssm-ID: 341082 Cd Length: 157 Bit Score: 239.53 E-value: 7.31e-73
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| STAT_bind | pfam02864 | STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ... |
336-469 | 1.34e-63 | |||||||||||
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. This family represents the DNA binding domain of STAT, which has an ig-like fold. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460727 Cd Length: 132 Bit Score: 212.06 E-value: 1.34e-63
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| STAT_alpha | pfam01017 | STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ... |
145-324 | 1.80e-59 | |||||||||||
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460026 Cd Length: 167 Bit Score: 201.68 E-value: 1.80e-59
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| STAT6_DBD | cd16850 | DNA-binding domain of Signal Transducer and Activator of Transcription 6 (STAT6); This family ... |
332-488 | 7.18e-59 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 6 (STAT6); This family consists of the DNA-binding domain (DBD) of the STAT6 proteins (Signal Transducer and Activator of Transcription 6, or Signal Transduction And Transcription 6). The DNA binding domain has an Ig-like fold. STAT6 is essential for the functional responses of T helper 2 (Th2) lymphocyte mediated by interleukins IL-4 and IL-13. STAT6 almost exclusively mediates the expression of genes activated by these cytokines; IL-4 signaling regulates the expression of genes involved in immune and anti-inflammatory responses. Abnormal production of IL-4 and IL-13 play important roles in the pathogenesis of asthma where upregulation of the Th2 response mediated by IL-4/IL-13 is a main characteristic. STAT6 has a unique extended transactivation domain, not found in other STATs, through which it recruits p300/CBP and NCoA-1, two coactivators needed for transcriptional activation by IL-4. STAT6 activation is linked to Kaposi's sarcoma-associated herpesvirus (KSHV)-associated cancers such as primary effusion lymphoma, a cancerous proliferation of B cells. Studies show that Meningeal solitary fibrous tumor (SFT) and hemangiopericytoma (HPC) represent a histopathologic spectrum linked by STAT6 nuclear expression and recurrent somatic fusions of the two genes, NGFI-A-binding protein 2 (NAB2) and STAT6 (NAB2-STAT6), similar to their soft tissue counterparts. It is associated with local recurrence and late distance metastasis of brain tumors to extracranial sites. Pssm-ID: 341088 Cd Length: 160 Bit Score: 199.72 E-value: 7.18e-59
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| SH2_STAT_family | cd09919 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-685 | 1.68e-54 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) family; STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated by a receptor. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. The CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198175 Cd Length: 115 Bit Score: 185.48 E-value: 1.68e-54
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| STAT_int | pfam02865 | STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ... |
2-124 | 5.73e-53 | |||||||||||
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017. Pssm-ID: 460728 Cd Length: 119 Bit Score: 181.26 E-value: 5.73e-53
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| STAT_int | smart00964 | STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ... |
2-125 | 4.28e-49 | |||||||||||
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain. Pssm-ID: 214942 Cd Length: 120 Bit Score: 170.16 E-value: 4.28e-49
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| SH2_STAT6 | cd10377 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 ... |
573-700 | 5.57e-49 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 proteins; STAT6 mediate signals from the IL-4 receptor. Unlike the other STAT proteins which bind an IFNgamma Activating Sequence (GAS), STAT6 stands out as having a unique binding site preference. This site consists of a palindromic sequence separated by a 3 bp spacer (TTCNNNG-AA)(N3 site). STAT6 is able to bind the GAS site but only at a low affinity. STAT6 may be an important regulator of mitogenesis when cells respond normally to IL-4. There is speculation that the inappropriate activation of STAT6 is involved in uncontrolled cell growth in an oncogenic state. IFNgamma is a negative regulator of STAT6 dependent transcription of target genes. Bcl-6 is another negative regulator of STAT6 activity. Bcl-6 is a transcriptional repressor normally expressed in germinal center B cells and some T cells. IL-4 signaling via STAT6 initially occurs unopposed, but is then dampened by a negative feedback mechanism through the IL-4/Stat6 dependent induction of SOCS1 expression. The IL-4 dependent aspect of Th2 differentiation requires the activation of STAT6. IL-4 signaling and STAT6 appear to play an important role in the immune response. Recently, it was shown that large scale chromatin remodeling of the IL-4 gene occurs as cells differentiate into Th2 effectors is STAT6 dependent. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198240 Cd Length: 129 Bit Score: 170.36 E-value: 5.57e-49
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| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
755-1187 | 1.03e-44 | |||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 165.47 E-value: 1.03e-44
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| PRK11107 | PRK11107 | hybrid sensory histidine kinase BarA; Provisional |
827-1470 | 1.22e-43 | |||||||||||
hybrid sensory histidine kinase BarA; Provisional Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 173.11 E-value: 1.22e-43
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| REC_hyHK_CKI1_RcsC-like | cd17546 | phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
1350-1466 | 1.81e-41 | |||||||||||
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 148.00 E-value: 1.81e-41
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| WalK | COG5002 | Sensor histidine kinase WalK [Signal transduction mechanisms]; |
830-1189 | 4.23e-37 | |||||||||||
Sensor histidine kinase WalK [Signal transduction mechanisms]; Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 145.08 E-value: 4.23e-37
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| KdpD | COG2205 | K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
827-1189 | 1.14e-36 | |||||||||||
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 138.89 E-value: 1.14e-36
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| CheY | COG0784 | CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
1347-1475 | 2.26e-35 | |||||||||||
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms]; Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 131.13 E-value: 2.26e-35
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| HATPase_EvgS-ArcB-TorS-like | cd16922 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
1112-1186 | 6.79e-34 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 126.45 E-value: 6.79e-34
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| PRK15347 | PRK15347 | two component system sensor kinase; |
748-1474 | 3.21e-33 | |||||||||||
two component system sensor kinase; Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 139.78 E-value: 3.21e-33
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| STAT_CCD | cd14786 | Coiled-coil domain of Signal Transducer and Activator of Transcription (STAT), also called ... |
212-328 | 1.19e-31 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription (STAT), also called alpha domain; This family consists of the coiled-coil (alpha) domain of the STAT proteins (Signal Transducer and Activator of Transcription, or Signal Transduction And Transcription), which are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. STAT proteins regulate several aspects of growth, survival and differentiation in cells. The transcription factors of this family are activated by JAK (Janus kinase) and dysregulation of this pathway is frequently observed in primary tumors and leads to immunosuppression, increased angiogenesis and enhanced survival of tumors. There are seven mammalian STAT family members that have been identified: STAT1, STAT2, STAT3, STAT4, STAT5A, STAT5B and STAT6. STAT proteins consist of six structural regions: N-domain (ND)/protein interaction domain, coiled-coil domain (CCD)/STAT all alpha domain, DNA-binding domain (DBD), linker domain (LK), a Src homology 2 (SH2) domain, and C-terminal transcriptional activation domain (TA) that includes two conserved phosphorylation sites (tyrosine and serine residues). The coiled-coil or alpha domain is an interacting region with other proteins, including IRF-9/p48 for STAT1, c-Jun, StIP1, and GRIM-19 for STAT3, and SMRT with STAT5A and STAT5B. A functional STAT1 mutant (phenylalanine to serine) in this domain region shows significantly decreased protein expression caused by translational/post-translational mechanisms independent of proteasome machinery. The phenylalanine is not conserved in STAT4 and STAT6 that have tight specificity, suggesting a novel potential mechanism of specific activation of STAT proteins. Specifically, STAT3, STAT5, and STAT6, which are continually imported to the nucleus independent of tyrosine phosphorylation, require the conformational structure of their coiled-coil domains. Pssm-ID: 341075 Cd Length: 125 Bit Score: 120.48 E-value: 1.19e-31
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| Response_reg | pfam00072 | Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
1350-1466 | 1.82e-31 | |||||||||||
Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain. Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 119.56 E-value: 1.82e-31
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| SH2_STAT4 | cd10375 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ... |
573-704 | 3.70e-28 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 4proteins; STAT4 mediate signals from the IL-12 receptors. STAT4 is mainly phosphorylated by IL-12-mediated signaling pathway in T cells. STAT4 expression is restricted in myeloid cells, thymus and testis. L-12 is the major cytokine that can activate STAT4, resulting in its tyrosine phosphorylation. The IL-12 receptor has two chains, termed IL-12R 1 and IL-12R 2, and ligand binding results in heterodimer formation and activation of the receptor associated JAK kinases, Jak2 and Tyk2. Phosphorylated STAT4 homo-dimerizes via its SH2 domain, and translocates into nucleus where it can recognize traditional N3 STAT target sequences in IL-12 responsive genes. STAT4 can also be phosphorylated in response to IFN-gamma stimulation through activation of Jak1 and Tyk2 in human. IL-17 can also activate STAT4 in human monocytic leukemia cell lines and IL-2 can induce Jak2 and Stat4 activation in NK cells but not in T cells. T helper 1 (Th1) cells produce IL-2 and IFNgamma, whereas Th2 cells secrete IL-4, IL-5, IL-6 and IL-13. Th1 cells are responsible for cell-mediated/inflammatory immunity and can enhance defenses against infectious agents and cancer, while Th2 cells are essential for humoral immunity and the clearance of parasitic antigens. The most potent factors that can promote Th1 and Th2 differentiation are the cytokines IL-12 and IL-4 respectively Although STAT4 is expressed both in Th1 and Th2 cells, STAT4 can only be phosphorylated by IL-12 which suggests that STAT4 plays an important role in Th1 cell function or development. STAT4 activation leads to Th1 differentiation, including the target genes of STAT4 such as ERM, a transcription factor that belongs to the Ets family of transcription factors. The expression of ERM is specifically induced by IL-12 in wild-type Th1 cells, but not in STAT4-deficient T cells. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198238 Cd Length: 148 Bit Score: 111.51 E-value: 3.70e-28
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| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
1113-1186 | 3.08e-27 | |||||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 107.35 E-value: 3.08e-27
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| PleD | COG3706 | Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
1349-1475 | 9.18e-27 | |||||||||||
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription]; Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 108.46 E-value: 9.18e-27
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| SH2_STAT3 | cd10374 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 ... |
563-705 | 2.86e-25 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 proteins; STAT3 encoded by this gene is a member of the STAT protein family. STAT3 mediates the expression of a variety of genes in response to cell stimuli, and plays a key role in many cellular processes such as cell growth and apoptosis. The small GTPase Rac1 regulates the activity of STAT3 and PIAS3 inhibits it. Three alternatively spliced transcript variants encoding distinct isoforms have been described. STAT 3 activation is required for self-renewal of embryonic stem cells (ESCs) and is essential for the differentiation of the TH17 helper T cells. Mutations in the STAT3 gene result in Hyperimmunoglobulin E syndrome and human cancers. STAT3 has been shown to interact with Androgen receptor, C-jun, ELP2, EP300, Epidermal growth factor receptor, Glucocorticoid receptor, HIF1A, Janus kinase 1, KHDRBS1, Mammalian target of rapamycin, MyoD, NDUFA13, NFKB1, Nuclear receptor coactivator 1, Promyelocytic leukemia protein, RAC1, RELA, RET proto-oncogene, RPA2, Src, STAT1, and TRIP10. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198237 Cd Length: 162 Bit Score: 103.57 E-value: 2.86e-25
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| PRK10841 | PRK10841 | two-component system sensor histidine kinase RcsC; |
1113-1469 | 6.96e-25 | |||||||||||
two-component system sensor histidine kinase RcsC; Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 112.76 E-value: 6.96e-25
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| TMAO_torS | TIGR02956 | TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
747-1479 | 1.53e-24 | |||||||||||
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems] Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 111.79 E-value: 1.53e-24
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| SH2_STAT1 | cd10372 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 ... |
573-704 | 3.13e-24 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 proteins; STAT1 is a member of the STAT family of transcription factors. STAT1 is involved in upregulating genes due to a signal by interferons. STAT1 forms homodimers or heterodimers with STAT3 that bind to the Interferon-Gamma Activated Sequence (GAS) promoter element in response to IFN-gamma stimulation. STAT1 forms a heterodimer with STAT2 that can bind Interferon Stimulated Response Element (ISRE) promoter element in response to either IFN-alpha or IFN-beta stimulation. Binding in both cases leads to an increased expression of ISG (Interferon Stimulated Genes). STAT1 has been shown to interact with protein kinase R, Src, IRF1, STAT3, MCM5, STAT2, CD117, Fanconi anemia, complementation group C, CREB-binding protein, Interleukin 27 receptor, alpha subunit, PIAS1, BRCA1, Epidermal growth factor receptor, PTK2, Mammalian target of rapamycin, IFNAR2, PRKCD, TRADD, C-jun, Calcitriol receptor, ISGF3G, and GNB2L1. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198235 Cd Length: 151 Bit Score: 100.37 E-value: 3.13e-24
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| REC_DivK-like | cd17548 | phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ... |
1349-1457 | 1.24e-23 | |||||||||||
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381100 [Multi-domain] Cd Length: 115 Bit Score: 97.23 E-value: 1.24e-23
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| OmpR | COG0745 | DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
1349-1462 | 1.38e-23 | |||||||||||
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription]; Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 100.03 E-value: 1.38e-23
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| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
1113-1188 | 9.98e-23 | |||||||||||
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 94.36 E-value: 9.98e-23
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| YesN | COG4753 | Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ... |
1349-1456 | 5.22e-22 | |||||||||||
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 443786 [Multi-domain] Cd Length: 103 Bit Score: 92.14 E-value: 5.22e-22
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| REC | cd00156 | phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
1351-1456 | 3.73e-21 | |||||||||||
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 89.59 E-value: 3.73e-21
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| PRK11466 | PRK11466 | hybrid sensory histidine kinase TorS; Provisional |
753-1186 | 1.30e-20 | |||||||||||
hybrid sensory histidine kinase TorS; Provisional Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 98.82 E-value: 1.30e-20
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| RpfG | COG3437 | Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
1349-1466 | 4.08e-20 | |||||||||||
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms]; Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 90.61 E-value: 4.08e-20
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| CitB | COG4565 | DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
1349-1474 | 4.97e-20 | |||||||||||
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms]; Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 87.72 E-value: 4.97e-20
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| REC_ETR-like | cd19933 | phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ... |
1348-1466 | 6.68e-20 | |||||||||||
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381160 [Multi-domain] Cd Length: 117 Bit Score: 86.68 E-value: 6.68e-20
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| PRK11091 | PRK11091 | aerobic respiration control sensor protein ArcB; Provisional |
827-1469 | 1.09e-19 | |||||||||||
aerobic respiration control sensor protein ArcB; Provisional Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 95.78 E-value: 1.09e-19
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| SH2_STAT2 | cd10373 | Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ... |
573-683 | 3.15e-19 | |||||||||||
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 proteins; STAT2 is a member of the STAT protein family. In response to interferon, STAT2 forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with STAT2, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. STAT2 has been shown to interact with MED14, CREB-binding protein, SMARCA4, STAT1, IFNAR2, IFNAR1, and ISGF3G. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198236 Cd Length: 151 Bit Score: 86.10 E-value: 3.15e-19
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| COG4191 | COG4191 | Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1113-1186 | 4.52e-19 | |||||||||||
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms]; Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 90.63 E-value: 4.52e-19
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| STAT3_CCD | cd16853 | Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
139-307 | 6.10e-19 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment. Pssm-ID: 341078 [Multi-domain] Cd Length: 180 Bit Score: 86.20 E-value: 6.10e-19
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| NtrB | COG3852 | Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
1112-1191 | 6.62e-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: 6.62e-19
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| COG4251 | COG4251 | Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
1106-1189 | 7.82e-19 | |||||||||||
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms]; Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 91.77 E-value: 7.82e-19
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| REC_D1_PleD-like | cd17538 | first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ... |
1349-1457 | 1.08e-18 | |||||||||||
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381093 [Multi-domain] Cd Length: 104 Bit Score: 82.55 E-value: 1.08e-18
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| AmiR | COG3707 | Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
1349-1466 | 2.05e-18 | |||||||||||
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 85.01 E-value: 2.05e-18
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| REC_OmpR | cd17574 | phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
1351-1456 | 3.60e-18 | |||||||||||
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 80.91 E-value: 3.60e-18
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| REC_NarL-like | cd17535 | phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ... |
1350-1455 | 1.91e-17 | |||||||||||
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381090 [Multi-domain] Cd Length: 117 Bit Score: 79.48 E-value: 1.91e-17
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| REC_CheY_CheY3 | cd19923 | phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ... |
1348-1466 | 2.95e-17 | |||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 79.30 E-value: 2.95e-17
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| REC_CheY | cd17542 | phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ... |
1348-1462 | 5.73e-17 | |||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381097 [Multi-domain] Cd Length: 117 Bit Score: 78.09 E-value: 5.73e-17
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| STAT4_DBD | cd16848 | DNA-binding domain of Signal Transducer and Activator of Transcription 4 (STAT4); This family ... |
332-486 | 5.75e-17 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 4 (STAT4); This family consists of the DNA-binding domain (DBD) of the STAT4 proteins (Signal Transducer and Activator of Transcription 4, or Signal Transduction And Transcription 4). The DNA binding domain has an Ig-like fold. STAT4 acts as the major signaling transducing STATs in response to interleukin-12 (IL-12) by inducing interferon-gamma (IFNg) , and is a central mediator in generating inflammation during protective immune responses and immune-mediated diseases. STAT4 is a critical regulator of Th1 differentiation and inflammatory disease. It is essential for the differentiation and function of many immune cells, including natural killer cells, dendritic cells, mast cells and T helper cells. STAT4-mediated signaling promotes the production of autoimmune-associated components, which are implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis and psoriasis, making STAT4 a promising therapeutic target for autoimmune diseases. Variations in STAT4 gene are linked to the development of systemic lupus erythematosus (SLE) in humans. STAT4 activation is detected in chronic liver diseases; polymorphism in STAT4 gene has been shown to be associated with the antiviral response in primary biliary cirrhosis (PBC), HCV-associated liver fibrosis, hepatocellular carcinoma (HCC), chronic hepatitis C and in drug-induced liver injury (DILI). STAT4 may inhibit HCC development by modulating HCC cell proliferation. Studies show that increased expression of STAT4 is positively correlated with the depth of invasion in colorectal cancer (CRC) patients, and the growth and invasion of CRC cells are repressed by inhibition of STAT4 expression, making STAT4 a promising therapeutic target for the treatment of CRC. Pssm-ID: 341086 Cd Length: 152 Bit Score: 79.68 E-value: 5.75e-17
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| AtoC | COG2204 | DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
1346-1480 | 8.22e-17 | |||||||||||
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms]; Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 84.63 E-value: 8.22e-17
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| REC_RpfG-like | cd17551 | phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
1349-1464 | 2.86e-16 | |||||||||||
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381103 [Multi-domain] Cd Length: 118 Bit Score: 76.33 E-value: 2.86e-16
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| REC_DC-like | cd17534 | phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ... |
1349-1466 | 3.86e-16 | |||||||||||
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381089 [Multi-domain] Cd Length: 117 Bit Score: 75.91 E-value: 3.86e-16
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| REC_2_DhkD-like | cd17580 | second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
1350-1457 | 2.66e-15 | |||||||||||
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 73.26 E-value: 2.66e-15
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| HATPase_AtoS-like | cd16943 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1186 | 2.79e-15 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains. Pssm-ID: 340419 [Multi-domain] Cd Length: 105 Bit Score: 73.23 E-value: 2.79e-15
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| REC_CheY4-like | cd17562 | phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ... |
1349-1462 | 5.25e-15 | |||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381110 [Multi-domain] Cd Length: 118 Bit Score: 72.72 E-value: 5.25e-15
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| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
1113-1186 | 5.56e-15 | |||||||||||
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: 79.24 E-value: 5.56e-15
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| HATPase_TutC-TodS-like | cd16925 | Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
1078-1185 | 5.82e-15 | |||||||||||
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain. Pssm-ID: 340402 [Multi-domain] Cd Length: 110 Bit Score: 72.14 E-value: 5.82e-15
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| KinE | COG5809 | Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
1112-1195 | 6.60e-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: 6.60e-15
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| HATPase_RstB-like | cd16939 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1186 | 6.61e-15 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain. Pssm-ID: 340416 [Multi-domain] Cd Length: 104 Bit Score: 72.08 E-value: 6.61e-15
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| HATPase_TmoS-FixL-DctS-like | cd16920 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1113-1185 | 9.24e-15 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340397 [Multi-domain] Cd Length: 104 Bit Score: 71.66 E-value: 9.24e-15
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| REC_PdtaR-like | cd19932 | phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ... |
1348-1462 | 9.96e-15 | |||||||||||
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381159 [Multi-domain] Cd Length: 118 Bit Score: 72.06 E-value: 9.96e-15
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| PRK10604 | PRK10604 | sensor protein RstB; Provisional |
1115-1190 | 1.56e-14 | |||||||||||
sensor protein RstB; Provisional Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 77.72 E-value: 1.56e-14
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| HATPase_FilI-like | cd16921 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1105-1185 | 2.30e-14 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340398 [Multi-domain] Cd Length: 105 Bit Score: 70.43 E-value: 2.30e-14
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| PRK11360 | PRK11360 | two-component system sensor histidine kinase AtoS; |
1096-1187 | 8.79e-14 | |||||||||||
two-component system sensor histidine kinase AtoS; Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 76.16 E-value: 8.79e-14
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| REC_YesN-like | cd17536 | phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ... |
1350-1468 | 1.02e-13 | |||||||||||
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381091 [Multi-domain] Cd Length: 121 Bit Score: 68.90 E-value: 1.02e-13
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| REC_Rcp-like | cd17557 | phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ... |
1349-1457 | 1.70e-13 | |||||||||||
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381108 [Multi-domain] Cd Length: 129 Bit Score: 68.60 E-value: 1.70e-13
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| REC_CheB-like | cd17541 | phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ... |
1348-1456 | 2.25e-13 | |||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381096 [Multi-domain] Cd Length: 125 Bit Score: 68.19 E-value: 2.25e-13
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| STAT1_DBD | cd16845 | DNA-binding domain of Signal Transducer and Activator of Transcription 1 (STAT1); This family ... |
332-486 | 2.28e-13 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 1 (STAT1); This family consists of the DNA-binding domain (DBD) of the STAT1 proteins (Signal Transducer and Activator of Transcription 1, or Signal Transduction And Transcription 1). The DNA binding domain has an Ig-like fold. STAT1 plays an essential role in mediating responses to all types of interferons (IFN), transducing signals from cytoplasmic domains of transmembrane receptors into the nucleus where it regulates gene expression. Thus STAT1 is involved in modulating diverse cellular processes, such as antimicrobial activities, cell proliferation and cell death. STAT1 function is crucial in the innate and adaptive arm of immunity and protects from pathogen infections; phosphorylation of a critical tyrosine by Janus kinases (JAKs) leads to its activation and nuclear translocation, while phosphorylation of a critical serine is required for full transcriptional activation upon IFN stimulation and in response to cellular stress. Transcription of protein-encoding genes (including Stat1 itself) as well as expression of microRNAs (miRNAs) is regulated by activated STAT1. Animal studies have shown that STAT1 is generally considered a tumor suppressor but it can also act as a tumor promoter; its functions are not restricted to tumor cells, but extend to parts of the tumor microenvironment such as immune cells, endothelial cells. STAT1 abundance is a reliable marker for good prognosis in selected tumor types, but it can also correlate with disease progression. In head and neck cancer (HNC) patients, upregulation of STAT1-induced HLA class I enhances immunogenicity and clinical response to anti-EGFR mAb cetuximab therapy. In systemic juvenile idiopathic arthritis (sJIA) characterized by systemic inflammation and arthritis, STAT1 phosphorylation downstream of IFNs is impaired. It exerts anti-oncogenic activities through interferon-gamma and interferon-alpha. STAT1 may inhibit hepatocellular carcinoma cell growth by regulating p53-related cell cycling and apoptosis. Studies also show a significant correlation of high STAT1 activity with longer colorectal cancer patient overall survival. Recent studies have shown that STAT1 suppresses mouse mammary gland tumorigenesis by immune regulatory as well as tumor cell-specific functions of STAT1. Pssm-ID: 341083 Cd Length: 161 Bit Score: 69.51 E-value: 2.28e-13
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| STAT1_CCD | cd16851 | Coiled-coil domain of Signal Transducer and Activator of Transcription 1 (STAT1); This family ... |
156-303 | 2.35e-13 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 1 (STAT1); This family consists of the coiled-coil (alpha) domain of the STAT1 proteins (Signal Transducer and Activator of Transcription 1, or Signal Transduction And Transcription 1). STAT1 plays an essential role in mediating responses to all types of interferons (IFN), transducing signals from cytoplasmic domains of transmembrane receptors into the nucleus where it regulates gene expression. Thus STAT1 is involved in modulating diverse cellular processes, such as antimicrobial activities, cell proliferation and cell death. STAT1 function is crucial in the innate and adaptive arm of immunity and protects from pathogen infections; phosphorylation of a critical tyrosine by Janus kinases (JAKs) leads to its activation and nuclear translocation, while phosphorylation of a critical serine is required for full transcriptional activation upon IFN stimulation and in response to cellular stress. Transcription of protein-encoding genes (including Stat1 itself) as well as expression of microRNAs (miRNAs) is regulated by activated STAT1. Animal studies have shown that STAT1 is generally considered a tumor suppressor but it can also act as a tumor promoter; its functions are not restricted to tumor cells, but extend to parts of the tumor microenvironment such as immune cells, endothelial cells. STAT1 abundance is a reliable marker for good prognosis in selected tumor types, but it can also correlate with disease progression. In head and neck cancer (HNC) patients, upregulation of STAT1-induced HLA class I enhances immunogenicity and clinical response to anti-EGFR mAb cetuximab therapy. In systemic juvenile idiopathic arthritis (sJIA) characterized by systemic inflammation and arthritis, STAT1 phosphorylation downstream of IFNs is impaired. It exerts anti-oncogenic activities through interferon-gamma and interferon-alpha. STAT1 may inhibit hepatocellular carcinoma cell growth by regulating p53-related cell cycling and apoptosis. Studies also show a significant correlation of high STAT1 activity with longer colorectal cancer patient overall survival. Recent studies have shown that STAT1 suppresses mouse mammary gland tumorigenesis by immune regulatory as well as tumor cell-specific functions of STAT1. Pssm-ID: 341076 Cd Length: 176 Bit Score: 69.81 E-value: 2.35e-13
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| SH2 | pfam00017 | SH2 domain; |
589-668 | 4.29e-13 | |||||||||||
SH2 domain; Pssm-ID: 425423 [Multi-domain] Cd Length: 77 Bit Score: 65.70 E-value: 4.29e-13
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| HATPase_EnvZ-like | cd16950 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1113-1185 | 5.02e-13 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain. Pssm-ID: 340426 [Multi-domain] Cd Length: 101 Bit Score: 66.32 E-value: 5.02e-13
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| STAT6_CCD | cd16856 | Coiled-coil domain of Signal Transducer and Activator of Transcription 6 (STAT6); This family ... |
136-335 | 1.73e-12 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 6 (STAT6); This family consists of the coiled-coil (alpha) domain of the STAT6 proteins (Signal Transducer and Activator of Transcription 6, or Signal Transduction And Transcription 6). SImilar to STAT3 and STAT5. the coiled-coil domain (CCD) of STAT6 is required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells.STAT6 is essential for the functional responses of T helper 2 (Th2) lymphocyte mediated by interleukins IL-4 and IL-13. STAT6 almost exclusively mediates the expression of genes activated by these cytokines; IL-4 signaling regulates the expression of genes involved in immune and anti-inflammatory responses. Abnormal production of IL-4 and IL-13 play important roles in the pathogenesis of asthma where upregulation of the Th2 response mediated by IL-4/IL-13 is a main characteristic. STAT6 has a unique extended transactivation domain, not found in other STATs, through which it recruits p300/CBP and NCoA-1, two coactivators needed for transcriptional activation by IL-4. STAT6 activation is linked to Kaposi's sarcoma-associated herpesvirus (KSHV)-associated cancers such as primary effusion lymphoma, a cancerous proliferation of B cells. Studies show that Meningeal solitary fibrous tumor (SFT) and hemangiopericytoma (HPC) represent a histopathologic spectrum linked by STAT6 nuclear expression and recurrent somatic fusions of the two genes, NGFI-A-binding protein 2 (NAB2) and STAT6 (NAB2-STAT6), similar to their soft tissue counterparts. It is associated with local recurrence and late distance metastasis of brain tumors to extracranial sites. Pssm-ID: 341081 Cd Length: 167 Bit Score: 67.10 E-value: 1.73e-12
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| REC_CheV-like | cd19924 | phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ... |
1350-1456 | 3.55e-12 | |||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381151 [Multi-domain] Cd Length: 111 Bit Score: 64.32 E-value: 3.55e-12
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| STAT2_DBD | cd16846 | DNA-binding domain of Signal Transducer and Activator of Transcription 2 (STAT2); This family ... |
332-486 | 4.24e-12 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 2 (STAT2); This family consists of the DNA-binding domain (DBD) of the STAT2 proteins (Signal Transducer and Activator of Transcription 2, or Signal Transduction And Transcription 2). The DNA binding domain has an Ig-like fold. STAT2 activation is driven predominantly by only two classes of cell surface receptors: Type I and III interferon receptors, making it a unique STAT family of transcription factors. Thus, STAT2 plays a critical role in host defenses against viral infections since type I interferon (IFN-I) response inhibits viral replication, and sets the stage for the development of adaptive immunity; viruses target STAT2 by either inhibiting its expression, blocking its activity, or by targeting it for degradation, thus triggering remarkable divergence in the STAT2 gene across species compared to other STAT family members. STAT2 function is regulated by tyrosine phosphorylation which enables STAT dimerization, and subsequent nuclear translocation and transcriptional activation of IFN stimulated genes. Dengue virus (DENV)-mediated degradation of STAT2 has emerged as an important determinant of DENV pathogenesis and host tropism. This vector-borne flavivirus suppresses IFN1 signaling to replicate and cause disease in vertebrates via proteasome-dependent STAT2 degradation mediated by the nonstructural protein NS5 and its interaction partner UBR4, an E3 ubiquitin ligase. The mechanism of Zika virus (ZIKV) NS5 resembles DENV NS5 but through different mechanism - ZIKV does not require the UBR4 to induce STAT2 degradation. It has also been shown that the STAT2 and STAT4 genes are direct targets for transcription factor Oct-1 protein which is involved in the regulation of expression of genes of the JAK-STAT signaling pathway in the Namalwa Burkitt's lymphoma cell line. Pssm-ID: 341084 Cd Length: 160 Bit Score: 65.61 E-value: 4.24e-12
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| CitA | COG3290 | Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
1113-1187 | 8.92e-12 | |||||||||||
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms]; Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 68.72 E-value: 8.92e-12
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| REC | smart00448 | cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ... |
1349-1408 | 1.22e-11 | |||||||||||
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues. Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 61.05 E-value: 1.22e-11
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| PRK10610 | PRK10610 | chemotaxis protein CheY; |
1342-1468 | 1.24e-11 | |||||||||||
chemotaxis protein CheY; Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 63.45 E-value: 1.24e-11
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| HATPase_BaeS-like | cd16946 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1096-1185 | 1.35e-11 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain. Pssm-ID: 340422 [Multi-domain] Cd Length: 109 Bit Score: 62.87 E-value: 1.35e-11
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| HATPase_CpxA-like | cd16949 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1113-1186 | 1.62e-11 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain. Pssm-ID: 340425 [Multi-domain] Cd Length: 104 Bit Score: 62.34 E-value: 1.62e-11
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| STAT2_CCD | cd16852 | Coiled-coil domain of Signal Transducer and Activator of Transcription 2 (STAT2); This family ... |
141-324 | 1.66e-11 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 2 (STAT2); This family consists of the coiled-coil (alpha) domain of the STAT2 proteins (Signal Transducer and Activator of Transcription 2, or Signal Transduction And Transcription 2). STAT2 activation is driven predominantly by only two classes of cell surface receptors: Type I and III interferon receptors, making it a unique STAT family of transcription factors. It differs from other STAT family members in that it associates constitutively with a non-STAT protein, the interferon regulatory factor 9 (IRF9). The coiled-coil domain of STAT2 is necessary for binding the carboxyl terminus of IRF9, an association required for the constitutive nuclear import of unphosphorylated STAT2. STAT2 plays a critical role in host defenses against viral infections since type I interferon (IFN-I) response inhibits viral replication, and sets the stage for the development of adaptive immunity; viruses target STAT2 by either inhibiting its expression, blocking its activity, or by targeting it for degradation, thus triggering remarkable divergence in the STAT2 gene across species compared to other STAT family members. STAT2 function is regulated by tyrosine phosphorylation which enables STAT dimerization, and subsequent nuclear translocation and transcriptional activation of IFN stimulated genes. Dengue virus (DENV)-mediated degradation of STAT2 has emerged as an important determinant of DENV pathogenesis and host tropism. This vector-borne flavivirus suppresses IFN1 signaling to replicate and cause disease in vertebrates via proteasome-dependent STAT2 degradation mediated by the nonstructural protein NS5 and its interaction partner UBR4, an E3 ubiquitin ligase. The mechanism of Zika virus (ZIKV) NS5 resembles DENV NS5 but through different mechanism - ZIKV does not require the UBR4 to induce STAT2 degradation. It has also been shown that the STAT2 and STAT4 genes are direct targets for transcription factor Oct-1 protein which is involved in the regulation of expression of genes of the JAK-STAT signaling pathway in the Namalwa Burkitt's lymphoma cell line. Pssm-ID: 341077 Cd Length: 172 Bit Score: 64.34 E-value: 1.66e-11
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| REC_OmpR_MtrA-like | cd17626 | phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ... |
1349-1461 | 2.07e-11 | |||||||||||
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381141 [Multi-domain] Cd Length: 115 Bit Score: 62.49 E-value: 2.07e-11
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| HATPase_EcPhoR-like | cd16952 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1185 | 2.18e-11 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism. Pssm-ID: 340428 [Multi-domain] Cd Length: 108 Bit Score: 62.22 E-value: 2.18e-11
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| REC_OmpR_PrrA-like | cd17627 | phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ... |
1350-1456 | 2.19e-11 | |||||||||||
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381142 [Multi-domain] Cd Length: 116 Bit Score: 62.40 E-value: 2.19e-11
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| phoR | PRK11006 | phosphate regulon sensor histidine kinase PhoR; |
1116-1185 | 2.69e-11 | |||||||||||
phosphate regulon sensor histidine kinase PhoR; Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 67.73 E-value: 2.69e-11
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| REC_OmpR_YycF-like | cd17614 | phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ... |
1350-1456 | 4.69e-11 | |||||||||||
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381130 [Multi-domain] Cd Length: 115 Bit Score: 61.29 E-value: 4.69e-11
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| glnL | PRK11073 | nitrogen regulation protein NR(II); |
1115-1186 | 4.77e-11 | |||||||||||
nitrogen regulation protein NR(II); Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 66.26 E-value: 4.77e-11
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| REC_OmpR_CusR-like | cd19935 | phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ... |
1350-1456 | 5.18e-11 | |||||||||||
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381162 [Multi-domain] Cd Length: 100 Bit Score: 60.53 E-value: 5.18e-11
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| PRK09959 | PRK09959 | acid-sensing system histidine kinase EvgS; |
1112-1469 | 1.09e-10 | |||||||||||
acid-sensing system histidine kinase EvgS; Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 66.68 E-value: 1.09e-10
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| envZ | PRK09467 | osmolarity sensor protein; Provisional |
1115-1186 | 1.41e-10 | |||||||||||
osmolarity sensor protein; Provisional Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 65.32 E-value: 1.41e-10
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| KinA | COG5805 | Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
1113-1186 | 1.70e-10 | |||||||||||
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: 65.14 E-value: 1.70e-10
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| SH2 | smart00252 | Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ... |
596-636 | 1.79e-10 | |||||||||||
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae. Pssm-ID: 214585 [Multi-domain] Cd Length: 84 Bit Score: 58.78 E-value: 1.79e-10
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| HATPase_YcbM-like | cd16947 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1113-1184 | 2.17e-10 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA). Pssm-ID: 340423 [Multi-domain] Cd Length: 125 Bit Score: 59.83 E-value: 2.17e-10
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| HATPase_Glnl-NtrB-like | cd16918 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1112-1185 | 4.28e-10 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s). Pssm-ID: 340395 [Multi-domain] Cd Length: 109 Bit Score: 58.57 E-value: 4.28e-10
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| REC_OmpR_DrrD-like | cd17625 | phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ... |
1351-1462 | 4.66e-10 | |||||||||||
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381140 [Multi-domain] Cd Length: 115 Bit Score: 58.39 E-value: 4.66e-10
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| STAT4_CCD | cd16854 | Coiled-coil domain of Signal Transducer and Activator of Transcription 4 (STAT4); This family ... |
215-324 | 5.13e-10 | |||||||||||
Coiled-coil domain of Signal Transducer and Activator of Transcription 4 (STAT4); This family consists of the coiled-coil (alpha) domain of the STAT4 proteins (Signal Transducer and Activator of Transcription 4, or Signal Transduction And Transcription 4). STAT4 expression is restricted to spermatozoa, myeloid cells, and T lymphocytes, making it distinct from other STATs. It acts as the major signaling transducing STATs in response to interleukin-12 (IL-12) by inducing interferon-gamma (IFNgamma), and is a central mediator in generating inflammation during protective immune responses and immune-mediated diseases. STAT4 is a critical regulator of Th1 differentiation and inflammatory disease. It is essential for the differentiation and function of many immune cells, including natural killer cells, dendritic cells, mast cells and T helper cells. STAT4-mediated signaling promotes the production of autoimmune-associated components, which are implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis and psoriasis, making STAT4 a promising therapeutic target for autoimmune diseases. Variations in STAT4 gene are linked to the development of systemic lupus erythematosus (SLE) in humans. STAT4 activation is detected in chronic liver diseases; polymorphism in STAT4 gene has been shown to be associated with the antiviral response in primary biliary cirrhosis (PBC), HCV-associated liver fibrosis, hepatocellular carcinoma (HCC), chronic hepatitis C and in drug-induced liver injury (DILI). STAT4 may inhibit HCC development by modulating HCC cell proliferation. Studies show that increased expression of STAT4 is positively correlated with the depth of invasion in colorectal cancer (CRC) patients, and the growth and invasion of CRC cells are repressed by inhibition of STAT4 expression, making STAT4 a promising therapeutic target for the treatment of CRC. Pssm-ID: 341079 Cd Length: 173 Bit Score: 59.88 E-value: 5.13e-10
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| HATPase_DpiB-CitA-like | cd16915 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1185 | 9.46e-10 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain. Pssm-ID: 340392 [Multi-domain] Cd Length: 104 Bit Score: 57.30 E-value: 9.46e-10
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| REC_OmpR_BsPhoP-like | cd19937 | phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ... |
1351-1457 | 1.04e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381164 [Multi-domain] Cd Length: 116 Bit Score: 57.67 E-value: 1.04e-09
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| HATPase_BasS-like | cd16940 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1097-1177 | 1.32e-09 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain. Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 57.03 E-value: 1.32e-09
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| cpxA | PRK09470 | envelope stress sensor histidine kinase CpxA; |
1113-1190 | 1.50e-09 | |||||||||||
envelope stress sensor histidine kinase CpxA; Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 62.26 E-value: 1.50e-09
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| REC_PA4781-like | cd19920 | phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ... |
1350-1457 | 1.78e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381147 [Multi-domain] Cd Length: 103 Bit Score: 56.37 E-value: 1.78e-09
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| REC_TrrA-like | cd17554 | phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ... |
1349-1437 | 2.40e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381106 [Multi-domain] Cd Length: 113 Bit Score: 56.46 E-value: 2.40e-09
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| STAT3_DBD | cd16847 | DNA-binding domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
332-486 | 3.41e-09 | |||||||||||
DNA-binding domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the DNA-binding domain (DBD) of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). The DNA binding domain has an Ig-like fold. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment. Pssm-ID: 341085 Cd Length: 164 Bit Score: 57.41 E-value: 3.41e-09
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| REC_citrate_TCS | cd19925 | phosphoacceptor receiver (REC) domain of citrate family two-component system response ... |
1348-1469 | 6.17e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381152 [Multi-domain] Cd Length: 118 Bit Score: 55.33 E-value: 6.17e-09
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| REC_typeB_ARR-like | cd17584 | phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ... |
1350-1465 | 7.23e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381121 [Multi-domain] Cd Length: 115 Bit Score: 54.94 E-value: 7.23e-09
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| REC_OmpR_EcPhoP-like | cd19934 | phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ... |
1350-1456 | 9.61e-09 | |||||||||||
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381161 [Multi-domain] Cd Length: 117 Bit Score: 54.60 E-value: 9.61e-09
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| LytT | COG3279 | DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ... |
1349-1437 | 1.20e-08 | |||||||||||
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms]; Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 57.13 E-value: 1.20e-08
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| REC_OmpR_PmrA-like | cd17624 | phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ... |
1350-1456 | 1.47e-08 | |||||||||||
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381139 [Multi-domain] Cd Length: 115 Bit Score: 54.03 E-value: 1.47e-08
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| orf27 | CHL00148 | Ycf27; Reviewed |
1343-1456 | 1.48e-08 | |||||||||||
Ycf27; Reviewed Pssm-ID: 214376 [Multi-domain] Cd Length: 240 Bit Score: 57.03 E-value: 1.48e-08
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| HATPase_CckA-like | cd16919 | Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
1113-1185 | 1.73e-08 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s). Pssm-ID: 340396 [Multi-domain] Cd Length: 116 Bit Score: 53.92 E-value: 1.73e-08
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| REC_OmpR_CpxR | cd17623 | phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ... |
1350-1456 | 2.20e-08 | |||||||||||
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381138 [Multi-domain] Cd Length: 115 Bit Score: 53.85 E-value: 2.20e-08
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| REC_hyHK | cd17598 | phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ... |
1350-1456 | 2.22e-08 | |||||||||||
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 53.87 E-value: 2.22e-08
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| PRK10490 | PRK10490 | sensor protein KdpD; Provisional |
1113-1192 | 2.36e-08 | |||||||||||
sensor protein KdpD; Provisional Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 58.89 E-value: 2.36e-08
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| REC_OmpR_PhoB | cd17618 | phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ... |
1349-1456 | 2.79e-08 | |||||||||||
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381133 [Multi-domain] Cd Length: 118 Bit Score: 53.41 E-value: 2.79e-08
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| REC_OmpR_kpRstA-like | cd17622 | phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ... |
1349-1462 | 8.17e-08 | |||||||||||
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381137 [Multi-domain] Cd Length: 116 Bit Score: 52.00 E-value: 8.17e-08
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| PRK10955 | PRK10955 | envelope stress response regulator transcription factor CpxR; |
1349-1456 | 8.20e-08 | |||||||||||
envelope stress response regulator transcription factor CpxR; Pssm-ID: 182864 [Multi-domain] Cd Length: 232 Bit Score: 54.81 E-value: 8.20e-08
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| SH2 | cd00173 | Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ... |
596-636 | 9.09e-08 | |||||||||||
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others. Pssm-ID: 198173 [Multi-domain] Cd Length: 79 Bit Score: 50.92 E-value: 9.09e-08
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| PRK13837 | PRK13837 | two-component system VirA-like sensor kinase; |
1115-1186 | 1.02e-07 | |||||||||||
two-component system VirA-like sensor kinase; Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 56.61 E-value: 1.02e-07
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| HisKA | pfam00512 | His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
827-872 | 1.19e-07 | |||||||||||
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases. Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 49.90 E-value: 1.19e-07
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| PRK10618 | PRK10618 | phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
1113-1186 | 1.37e-07 | |||||||||||
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 56.48 E-value: 1.37e-07
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| PRK09303 | PRK09303 | histidine kinase; |
1111-1185 | 1.37e-07 | |||||||||||
histidine kinase; Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 55.73 E-value: 1.37e-07
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| REC_DesR-like | cd19930 | phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ... |
1350-1455 | 1.83e-07 | |||||||||||
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381157 [Multi-domain] Cd Length: 117 Bit Score: 51.12 E-value: 1.83e-07
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| PRK10365 | PRK10365 | sigma-54-dependent response regulator transcription factor ZraR; |
1348-1474 | 3.33e-07 | |||||||||||
sigma-54-dependent response regulator transcription factor ZraR; Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 54.65 E-value: 3.33e-07
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| PRK00742 | PRK00742 | chemotaxis-specific protein-glutamate methyltransferase CheB; |
1348-1456 | 3.47e-07 | |||||||||||
chemotaxis-specific protein-glutamate methyltransferase CheB; Pssm-ID: 234828 [Multi-domain] Cd Length: 354 Bit Score: 54.00 E-value: 3.47e-07
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| PRK11361 | PRK11361 | acetoacetate metabolism transcriptional regulator AtoC; |
1349-1466 | 4.34e-07 | |||||||||||
acetoacetate metabolism transcriptional regulator AtoC; Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 54.08 E-value: 4.34e-07
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| REC_Ycf29 | cd19927 | phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ... |
1350-1456 | 4.63e-07 | |||||||||||
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381154 [Multi-domain] Cd Length: 102 Bit Score: 49.68 E-value: 4.63e-07
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| HATPase_ETR2_ERS2-EIN4-like | cd16938 | Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
1097-1184 | 7.19e-07 | |||||||||||
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 49.76 E-value: 7.19e-07
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| REC_CheC-like | cd17593 | phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ... |
1374-1469 | 7.29e-07 | |||||||||||
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381124 [Multi-domain] Cd Length: 117 Bit Score: 49.46 E-value: 7.29e-07
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| PRK11086 | PRK11086 | sensory histidine kinase DcuS; Provisional |
1114-1185 | 8.86e-07 | |||||||||||
sensory histidine kinase DcuS; Provisional Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 53.38 E-value: 8.86e-07
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| PRK11517 | PRK11517 | DNA-binding response regulator HprR; |
1348-1456 | 1.04e-06 | |||||||||||
DNA-binding response regulator HprR; Pssm-ID: 183172 [Multi-domain] Cd Length: 223 Bit Score: 51.44 E-value: 1.04e-06
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| Spo0A | COG5801 | Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ... |
1345-1456 | 1.15e-06 | |||||||||||
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444503 [Multi-domain] Cd Length: 264 Bit Score: 51.72 E-value: 1.15e-06
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| HATPase_HupT_MifS-like | cd16976 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1105-1184 | 1.63e-06 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain. Pssm-ID: 340435 [Multi-domain] Cd Length: 102 Bit Score: 47.84 E-value: 1.63e-06
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| PRK10755 | PRK10755 | two-component system sensor histidine kinase PmrB; |
1117-1171 | 1.87e-06 | |||||||||||
two-component system sensor histidine kinase PmrB; Pssm-ID: 236751 [Multi-domain] Cd Length: 356 Bit Score: 51.89 E-value: 1.87e-06
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| HisKA | smart00388 | His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
827-872 | 1.89e-06 | |||||||||||
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases. Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 46.79 E-value: 1.89e-06
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| REC_Spo0A | cd17561 | phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ... |
1348-1456 | 2.50e-06 | |||||||||||
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381109 [Multi-domain] Cd Length: 108 Bit Score: 47.60 E-value: 2.50e-06
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| HisKA | cd00082 | Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
830-872 | 3.03e-06 | |||||||||||
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: 46.05 E-value: 3.03e-06
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| phoR_proteo | TIGR02966 | phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ... |
830-969 | 3.77e-06 | |||||||||||
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems] Pssm-ID: 274368 [Multi-domain] Cd Length: 333 Bit Score: 50.67 E-value: 3.77e-06
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| PRK12555 | PRK12555 | chemotaxis-specific protein-glutamate methyltransferase CheB; |
1348-1421 | 4.03e-06 | |||||||||||
chemotaxis-specific protein-glutamate methyltransferase CheB; Pssm-ID: 237135 [Multi-domain] Cd Length: 337 Bit Score: 50.65 E-value: 4.03e-06
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| ompR | PRK09468 | osmolarity response regulator; Provisional |
1344-1456 | 4.70e-06 | |||||||||||
osmolarity response regulator; Provisional Pssm-ID: 181883 [Multi-domain] Cd Length: 239 Bit Score: 49.59 E-value: 4.70e-06
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| REC_OmpR_MtPhoP-like | cd17615 | phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ... |
1349-1456 | 6.58e-06 | |||||||||||
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381131 [Multi-domain] Cd Length: 118 Bit Score: 46.58 E-value: 6.58e-06
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| CitB | COG2197 | DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ... |
1348-1419 | 6.61e-06 | |||||||||||
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 441799 [Multi-domain] Cd Length: 131 Bit Score: 47.19 E-value: 6.61e-06
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| REC_OmpR_KdpE-like | cd17620 | phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ... |
1350-1456 | 8.32e-06 | |||||||||||
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381135 [Multi-domain] Cd Length: 99 Bit Score: 46.00 E-value: 8.32e-06
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| REC_RR468-like | cd17552 | phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ... |
1349-1462 | 8.57e-06 | |||||||||||
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381104 [Multi-domain] Cd Length: 121 Bit Score: 46.39 E-value: 8.57e-06
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| PRK13557 | PRK13557 | histidine kinase; Provisional |
1113-1191 | 1.11e-05 | |||||||||||
histidine kinase; Provisional Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 50.05 E-value: 1.11e-05
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| PRK10364 | PRK10364 | two-component system sensor histidine kinase ZraS; |
1113-1190 | 1.13e-05 | |||||||||||
two-component system sensor histidine kinase ZraS; Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 49.78 E-value: 1.13e-05
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| HATPase_BceS-YxdK-YvcQ-like | cd16948 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1185 | 1.49e-05 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds. Pssm-ID: 340424 [Multi-domain] Cd Length: 109 Bit Score: 45.35 E-value: 1.49e-05
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| PRK10643 | PRK10643 | two-component system response regulator PmrA; |
1349-1479 | 1.97e-05 | |||||||||||
two-component system response regulator PmrA; Pssm-ID: 182612 [Multi-domain] Cd Length: 222 Bit Score: 47.34 E-value: 1.97e-05
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| REC_LytTR_AlgR-like | cd17532 | phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ... |
1350-1435 | 2.56e-05 | |||||||||||
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381087 [Multi-domain] Cd Length: 118 Bit Score: 44.84 E-value: 2.56e-05
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| PRK09483 | PRK09483 | response regulator; Provisional |
1348-1455 | 2.79e-05 | |||||||||||
response regulator; Provisional Pssm-ID: 236538 [Multi-domain] Cd Length: 217 Bit Score: 47.02 E-value: 2.79e-05
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| REC_OmpR_ArcA_TorR-like | cd17619 | phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ... |
1350-1456 | 2.87e-05 | |||||||||||
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381134 [Multi-domain] Cd Length: 113 Bit Score: 44.69 E-value: 2.87e-05
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| PRK10549 | PRK10549 | two-component system sensor histidine kinase BaeS; |
1108-1187 | 3.25e-05 | |||||||||||
two-component system sensor histidine kinase BaeS; Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 48.09 E-value: 3.25e-05
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| REC_OmpR_CtrA | cd17616 | phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ... |
1350-1462 | 3.50e-05 | |||||||||||
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381132 [Multi-domain] Cd Length: 114 Bit Score: 44.71 E-value: 3.50e-05
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| REC_NtrX-like | cd17550 | phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ... |
1350-1462 | 3.85e-05 | |||||||||||
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381102 [Multi-domain] Cd Length: 115 Bit Score: 44.41 E-value: 3.85e-05
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| REC_OmpR_NsrR-like | cd18159 | phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ... |
1350-1466 | 5.15e-05 | |||||||||||
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381143 [Multi-domain] Cd Length: 113 Bit Score: 43.81 E-value: 5.15e-05
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| pleD | PRK09581 | response regulator PleD; Reviewed |
1347-1458 | 5.59e-05 | |||||||||||
response regulator PleD; Reviewed Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 47.59 E-value: 5.59e-05
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| HATPase_VanS-like | cd16923 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1112-1185 | 5.70e-05 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain. Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 43.53 E-value: 5.70e-05
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| HATPase_BvrS-ChvG-like | cd16953 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1113-1185 | 5.98e-05 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain. Pssm-ID: 340429 [Multi-domain] Cd Length: 110 Bit Score: 43.72 E-value: 5.98e-05
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| REC_RocR | cd17530 | phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ... |
1349-1471 | 1.48e-04 | |||||||||||
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381086 [Multi-domain] Cd Length: 123 Bit Score: 42.81 E-value: 1.48e-04
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| REC_2_GGDEF | cd17544 | second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ... |
1348-1456 | 1.68e-04 | |||||||||||
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381098 [Multi-domain] Cd Length: 122 Bit Score: 42.89 E-value: 1.68e-04
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| PRK11100 | PRK11100 | sensory histidine kinase CreC; Provisional |
1113-1186 | 1.79e-04 | |||||||||||
sensory histidine kinase CreC; Provisional Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 45.99 E-value: 1.79e-04
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| PRK15479 | PRK15479 | transcriptional regulator TctD; |
1349-1456 | 1.89e-04 | |||||||||||
transcriptional regulator TctD; Pssm-ID: 185376 [Multi-domain] Cd Length: 221 Bit Score: 44.33 E-value: 1.89e-04
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| YesM | COG2972 | Sensor histidine kinase YesM [Signal transduction mechanisms]; |
1113-1188 | 2.04e-04 | |||||||||||
Sensor histidine kinase YesM [Signal transduction mechanisms]; Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 45.78 E-value: 2.04e-04
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| PRK10651 | PRK10651 | transcriptional regulator NarL; Provisional |
1344-1455 | 2.18e-04 | |||||||||||
transcriptional regulator NarL; Provisional Pssm-ID: 182619 [Multi-domain] Cd Length: 216 Bit Score: 44.25 E-value: 2.18e-04
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
29-243 | 2.42e-04 | |||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.42e-04
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| REC_OmpR_BfmR-like | cd19939 | phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ... |
1349-1462 | 3.59e-04 | |||||||||||
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381166 [Multi-domain] Cd Length: 116 Bit Score: 41.59 E-value: 3.59e-04
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| HATPase_PhoQ-like | cd16954 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1115-1184 | 3.64e-04 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain. Pssm-ID: 340430 [Multi-domain] Cd Length: 135 Bit Score: 42.23 E-value: 3.64e-04
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| SH2_SH2D2A_SH2D7 | cd10349 | Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); ... |
596-627 | 4.29e-04 | |||||||||||
Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); SH2D2A and SH7 both contain a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 199830 Cd Length: 77 Bit Score: 40.20 E-value: 4.29e-04
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| cztS_silS_copS | TIGR01386 | heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
830-969 | 5.03e-04 | |||||||||||
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Pssm-ID: 273593 [Multi-domain] Cd Length: 457 Bit Score: 44.30 E-value: 5.03e-04
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| REC_typeA_ARR | cd17581 | phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ... |
1350-1458 | 6.68e-04 | |||||||||||
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381119 [Multi-domain] Cd Length: 122 Bit Score: 41.20 E-value: 6.68e-04
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| REC_CpdR_CckA-like | cd18160 | phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ... |
1349-1456 | 7.83e-04 | |||||||||||
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381144 [Multi-domain] Cd Length: 103 Bit Score: 40.56 E-value: 7.83e-04
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| pleD | PRK09581 | response regulator PleD; Reviewed |
1329-1457 | 7.89e-04 | |||||||||||
response regulator PleD; Reviewed Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 43.74 E-value: 7.89e-04
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| HATPase_SpaK_NisK-like | cd16975 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1079-1182 | 8.38e-04 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals. Pssm-ID: 340434 [Multi-domain] Cd Length: 107 Bit Score: 40.52 E-value: 8.38e-04
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| PRK09958 | PRK09958 | acid-sensing system DNA-binding response regulator EvgA; |
1351-1475 | 1.12e-03 | |||||||||||
acid-sensing system DNA-binding response regulator EvgA; Pssm-ID: 182168 [Multi-domain] Cd Length: 204 Bit Score: 41.80 E-value: 1.12e-03
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-303 | 1.22e-03 | |||||||||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.22e-03
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| REC_OmpR_VirG | cd17594 | phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ... |
1349-1462 | 1.24e-03 | |||||||||||
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381125 [Multi-domain] Cd Length: 113 Bit Score: 40.12 E-value: 1.24e-03
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| PRK10161 | PRK10161 | phosphate response regulator transcription factor PhoB; |
1349-1462 | 1.27e-03 | |||||||||||
phosphate response regulator transcription factor PhoB; Pssm-ID: 182277 [Multi-domain] Cd Length: 229 Bit Score: 42.01 E-value: 1.27e-03
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| REC_TrxB | cd17595 | phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ... |
1350-1476 | 1.30e-03 | |||||||||||
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381126 [Multi-domain] Cd Length: 135 Bit Score: 40.40 E-value: 1.30e-03
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| PRK09835 | PRK09835 | Cu(+)/Ag(+) sensor histidine kinase; |
830-971 | 1.49e-03 | |||||||||||
Cu(+)/Ag(+) sensor histidine kinase; Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 42.84 E-value: 1.49e-03
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| PRK09303 | PRK09303 | histidine kinase; |
831-970 | 1.49e-03 | |||||||||||
histidine kinase; Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 42.63 E-value: 1.49e-03
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| PRK11173 | PRK11173 | two-component response regulator; Provisional |
1349-1420 | 1.98e-03 | |||||||||||
two-component response regulator; Provisional Pssm-ID: 183013 [Multi-domain] Cd Length: 237 Bit Score: 41.54 E-value: 1.98e-03
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| REC_OmpR_RegX3-like | cd17621 | phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ... |
1350-1456 | 2.17e-03 | |||||||||||
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381136 [Multi-domain] Cd Length: 99 Bit Score: 39.10 E-value: 2.17e-03
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| HATPase_BasS-like | cd16940 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
939-970 | 2.85e-03 | |||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain. Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 38.93 E-value: 2.85e-03
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| SH2_Vav_family | cd09940 | Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several ... |
568-634 | 4.49e-03 | |||||||||||
Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, Vav2 and Vav3 are more ubiquitously expressed. The members here include insect and amphibian Vavs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198193 Cd Length: 102 Bit Score: 38.04 E-value: 4.49e-03
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| SH2_HSH2_like | cd09946 | Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function ... |
587-645 | 4.50e-03 | |||||||||||
Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function as an adapter protein involved in tyrosine kinase signaling. It may also be involved in regulating cytokine signaling and cytoskeletal reorganization in hematopoietic cells. HSH2 contains several putative protein-binding motifs, SH3-binding proline-rich regions, and phosphotyrosine sites, but lacks enzymatic motifs. HSH2 was found to interact with cytokine-regulated tyrosine kinase c-FES and an activated Cdc42-associated tyrosine kinase ACK1. HSH2 binds c-FES through both its C-terminal region and its N-terminal region including the SH2 domain and binds ACK1 via its N-terminal proline-rich region. Both kinases bound and tyrosine-phosphorylated HSH2 in mammalian cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198199 Cd Length: 102 Bit Score: 38.33 E-value: 4.50e-03
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| COG3920 | COG3920 | Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
1113-1191 | 4.74e-03 | |||||||||||
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]; Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 41.43 E-value: 4.74e-03
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| PRK09836 | PRK09836 | DNA-binding transcriptional activator CusR; Provisional |
1348-1456 | 4.82e-03 | |||||||||||
DNA-binding transcriptional activator CusR; Provisional Pssm-ID: 182102 [Multi-domain] Cd Length: 227 Bit Score: 40.29 E-value: 4.82e-03
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| psREC-like_D2_PleD | cd17539 | REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ... |
1350-1462 | 5.44e-03 | |||||||||||
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain. Pssm-ID: 381094 [Multi-domain] Cd Length: 124 Bit Score: 38.45 E-value: 5.44e-03
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| SH2_SH2D7 | cd10417 | Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a ... |
587-627 | 5.73e-03 | |||||||||||
Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 199832 Cd Length: 102 Bit Score: 37.95 E-value: 5.73e-03
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| REC_OmpR_BaeR-like | cd19938 | phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ... |
1349-1456 | 6.06e-03 | |||||||||||
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381165 [Multi-domain] Cd Length: 114 Bit Score: 38.13 E-value: 6.06e-03
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| COG4192 | COG4192 | Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1106-1172 | 7.17e-03 | |||||||||||
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms]; Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 40.83 E-value: 7.17e-03
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| DUF4686 | pfam15742 | Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
139-303 | 8.25e-03 | |||||||||||
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif. Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 8.25e-03
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| ComP | COG4585 | Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
1113-1189 | 8.95e-03 | |||||||||||
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 39.60 E-value: 8.95e-03
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