cysteine-rich repeat secretory protein, putative (DUF26) [Arabidopsis thaliana]
cysteine-rich repeat secretory family protein( domain architecture ID 10483325)
cysteine-rich repeat secretory family protein plays a role in salt stress response and has antifungal activity
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Stress-antifung | pfam01657 | Salt stress response/antifungal; This domain is often found in association with the kinase ... |
47-134 | 9.30e-21 | |||
Salt stress response/antifungal; This domain is often found in association with the kinase domains pfam00069 or pfam07714. In many proteins it is duplicated. It contains six conserved cysteines which are involved in disulphide bridges. It has a role in salt stress response and has antifungal activity. : Pssm-ID: 460284 Cd Length: 96 Bit Score: 84.05 E-value: 9.30e-21
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Gnk2-like | cd23509 | antifungal protein ginkbilobin-2-like domains found in plants; This family includes the ... |
153-261 | 2.42e-20 | |||
antifungal protein ginkbilobin-2-like domains found in plants; This family includes the antifungal protein ginkbilobin found in seeds of Ginkgo biloba. The full-length protein contains a signal peptide and is called ginkbilobin-2 (Gnk2 or stress-antifungal domain). Gnk2 is an extracellular domain harboring a conserved cysteine motif (C-8X-C-2X-C) in its core. This domain is present in three types of plant proteins: cysteine-rich receptor-like secreted proteins (CRRSPs), cysteine-rich receptor-like kinase (CRKs), and plasmodesmata-localized proteins (PDLPs). Gnk2 from Ginkgo biloba and maize AFP1 CRRSPs have been shown to bind mannose. CRKs that typically have two Gnk2 domains in the extracellular region, form part of a large subgroup of receptor-like protein kinases (RLKs) in plants and have been shown to participate in the control of stress responses and development in Arabidopsis. PDLPs contain two Gnk2 domains in their extracellular region and a transmembrane helix, but lack a kinase domain; they associate with plasmodesmata and are involved in symplastic intercellular signaling, pathogen response, systemic signaling, control of callose deposition and are targets for viral movement proteins. No ligand have been identified for PDLPs and CRKs. Although the precise biochemical functions of plant Gnk2 are not known, the conserved C-8X-C-2X-C motif may point to carbohydrate binding, similar to G. biloba Gnk2 inhibiting the growth of several fungi by binding mannose moieties of the fungal cell walls. : Pssm-ID: 467874 Cd Length: 100 Bit Score: 83.22 E-value: 2.42e-20
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Name | Accession | Description | Interval | E-value | |||
Stress-antifung | pfam01657 | Salt stress response/antifungal; This domain is often found in association with the kinase ... |
47-134 | 9.30e-21 | |||
Salt stress response/antifungal; This domain is often found in association with the kinase domains pfam00069 or pfam07714. In many proteins it is duplicated. It contains six conserved cysteines which are involved in disulphide bridges. It has a role in salt stress response and has antifungal activity. Pssm-ID: 460284 Cd Length: 96 Bit Score: 84.05 E-value: 9.30e-21
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Gnk2-like | cd23509 | antifungal protein ginkbilobin-2-like domains found in plants; This family includes the ... |
153-261 | 2.42e-20 | |||
antifungal protein ginkbilobin-2-like domains found in plants; This family includes the antifungal protein ginkbilobin found in seeds of Ginkgo biloba. The full-length protein contains a signal peptide and is called ginkbilobin-2 (Gnk2 or stress-antifungal domain). Gnk2 is an extracellular domain harboring a conserved cysteine motif (C-8X-C-2X-C) in its core. This domain is present in three types of plant proteins: cysteine-rich receptor-like secreted proteins (CRRSPs), cysteine-rich receptor-like kinase (CRKs), and plasmodesmata-localized proteins (PDLPs). Gnk2 from Ginkgo biloba and maize AFP1 CRRSPs have been shown to bind mannose. CRKs that typically have two Gnk2 domains in the extracellular region, form part of a large subgroup of receptor-like protein kinases (RLKs) in plants and have been shown to participate in the control of stress responses and development in Arabidopsis. PDLPs contain two Gnk2 domains in their extracellular region and a transmembrane helix, but lack a kinase domain; they associate with plasmodesmata and are involved in symplastic intercellular signaling, pathogen response, systemic signaling, control of callose deposition and are targets for viral movement proteins. No ligand have been identified for PDLPs and CRKs. Although the precise biochemical functions of plant Gnk2 are not known, the conserved C-8X-C-2X-C motif may point to carbohydrate binding, similar to G. biloba Gnk2 inhibiting the growth of several fungi by binding mannose moieties of the fungal cell walls. Pssm-ID: 467874 Cd Length: 100 Bit Score: 83.22 E-value: 2.42e-20
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Gnk2-like | cd23509 | antifungal protein ginkbilobin-2-like domains found in plants; This family includes the ... |
37-134 | 6.00e-18 | |||
antifungal protein ginkbilobin-2-like domains found in plants; This family includes the antifungal protein ginkbilobin found in seeds of Ginkgo biloba. The full-length protein contains a signal peptide and is called ginkbilobin-2 (Gnk2 or stress-antifungal domain). Gnk2 is an extracellular domain harboring a conserved cysteine motif (C-8X-C-2X-C) in its core. This domain is present in three types of plant proteins: cysteine-rich receptor-like secreted proteins (CRRSPs), cysteine-rich receptor-like kinase (CRKs), and plasmodesmata-localized proteins (PDLPs). Gnk2 from Ginkgo biloba and maize AFP1 CRRSPs have been shown to bind mannose. CRKs that typically have two Gnk2 domains in the extracellular region, form part of a large subgroup of receptor-like protein kinases (RLKs) in plants and have been shown to participate in the control of stress responses and development in Arabidopsis. PDLPs contain two Gnk2 domains in their extracellular region and a transmembrane helix, but lack a kinase domain; they associate with plasmodesmata and are involved in symplastic intercellular signaling, pathogen response, systemic signaling, control of callose deposition and are targets for viral movement proteins. No ligand have been identified for PDLPs and CRKs. Although the precise biochemical functions of plant Gnk2 are not known, the conserved C-8X-C-2X-C motif may point to carbohydrate binding, similar to G. biloba Gnk2 inhibiting the growth of several fungi by binding mannose moieties of the fungal cell walls. Pssm-ID: 467874 Cd Length: 100 Bit Score: 77.06 E-value: 6.00e-18
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Stress-antifung | pfam01657 | Salt stress response/antifungal; This domain is often found in association with the kinase ... |
210-260 | 8.59e-10 | |||
Salt stress response/antifungal; This domain is often found in association with the kinase domains pfam00069 or pfam07714. In many proteins it is duplicated. It contains six conserved cysteines which are involved in disulphide bridges. It has a role in salt stress response and has antifungal activity. Pssm-ID: 460284 Cd Length: 96 Bit Score: 54.77 E-value: 8.59e-10
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Name | Accession | Description | Interval | E-value | |||
Stress-antifung | pfam01657 | Salt stress response/antifungal; This domain is often found in association with the kinase ... |
47-134 | 9.30e-21 | |||
Salt stress response/antifungal; This domain is often found in association with the kinase domains pfam00069 or pfam07714. In many proteins it is duplicated. It contains six conserved cysteines which are involved in disulphide bridges. It has a role in salt stress response and has antifungal activity. Pssm-ID: 460284 Cd Length: 96 Bit Score: 84.05 E-value: 9.30e-21
|
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Gnk2-like | cd23509 | antifungal protein ginkbilobin-2-like domains found in plants; This family includes the ... |
153-261 | 2.42e-20 | |||
antifungal protein ginkbilobin-2-like domains found in plants; This family includes the antifungal protein ginkbilobin found in seeds of Ginkgo biloba. The full-length protein contains a signal peptide and is called ginkbilobin-2 (Gnk2 or stress-antifungal domain). Gnk2 is an extracellular domain harboring a conserved cysteine motif (C-8X-C-2X-C) in its core. This domain is present in three types of plant proteins: cysteine-rich receptor-like secreted proteins (CRRSPs), cysteine-rich receptor-like kinase (CRKs), and plasmodesmata-localized proteins (PDLPs). Gnk2 from Ginkgo biloba and maize AFP1 CRRSPs have been shown to bind mannose. CRKs that typically have two Gnk2 domains in the extracellular region, form part of a large subgroup of receptor-like protein kinases (RLKs) in plants and have been shown to participate in the control of stress responses and development in Arabidopsis. PDLPs contain two Gnk2 domains in their extracellular region and a transmembrane helix, but lack a kinase domain; they associate with plasmodesmata and are involved in symplastic intercellular signaling, pathogen response, systemic signaling, control of callose deposition and are targets for viral movement proteins. No ligand have been identified for PDLPs and CRKs. Although the precise biochemical functions of plant Gnk2 are not known, the conserved C-8X-C-2X-C motif may point to carbohydrate binding, similar to G. biloba Gnk2 inhibiting the growth of several fungi by binding mannose moieties of the fungal cell walls. Pssm-ID: 467874 Cd Length: 100 Bit Score: 83.22 E-value: 2.42e-20
|
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Gnk2-like | cd23509 | antifungal protein ginkbilobin-2-like domains found in plants; This family includes the ... |
37-134 | 6.00e-18 | |||
antifungal protein ginkbilobin-2-like domains found in plants; This family includes the antifungal protein ginkbilobin found in seeds of Ginkgo biloba. The full-length protein contains a signal peptide and is called ginkbilobin-2 (Gnk2 or stress-antifungal domain). Gnk2 is an extracellular domain harboring a conserved cysteine motif (C-8X-C-2X-C) in its core. This domain is present in three types of plant proteins: cysteine-rich receptor-like secreted proteins (CRRSPs), cysteine-rich receptor-like kinase (CRKs), and plasmodesmata-localized proteins (PDLPs). Gnk2 from Ginkgo biloba and maize AFP1 CRRSPs have been shown to bind mannose. CRKs that typically have two Gnk2 domains in the extracellular region, form part of a large subgroup of receptor-like protein kinases (RLKs) in plants and have been shown to participate in the control of stress responses and development in Arabidopsis. PDLPs contain two Gnk2 domains in their extracellular region and a transmembrane helix, but lack a kinase domain; they associate with plasmodesmata and are involved in symplastic intercellular signaling, pathogen response, systemic signaling, control of callose deposition and are targets for viral movement proteins. No ligand have been identified for PDLPs and CRKs. Although the precise biochemical functions of plant Gnk2 are not known, the conserved C-8X-C-2X-C motif may point to carbohydrate binding, similar to G. biloba Gnk2 inhibiting the growth of several fungi by binding mannose moieties of the fungal cell walls. Pssm-ID: 467874 Cd Length: 100 Bit Score: 77.06 E-value: 6.00e-18
|
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Stress-antifung | pfam01657 | Salt stress response/antifungal; This domain is often found in association with the kinase ... |
210-260 | 8.59e-10 | |||
Salt stress response/antifungal; This domain is often found in association with the kinase domains pfam00069 or pfam07714. In many proteins it is duplicated. It contains six conserved cysteines which are involved in disulphide bridges. It has a role in salt stress response and has antifungal activity. Pssm-ID: 460284 Cd Length: 96 Bit Score: 54.77 E-value: 8.59e-10
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Blast search parameters | ||||
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