FHA (forkhead-associated) domain-containing protein participates in signal transduction pathways via protein-protein interactions involving recognition of pThr and pTyr phosphopeptides| FOXK family forkhead box protein functions as a transcription factor, similar to FOXK1, one of the transcription factors managing the passage from the normal cellular respiration (complete glucose oxidation) to generating ATP and intermediaries for many other biochemical pathways
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain ...
162-416
7.17e-163
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
:
Pssm-ID: 293298 Cd Length: 254 Bit Score: 458.15 E-value: 7.17e-163
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
4-96
1.38e-29
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
The actual alignment was detected with superfamily member cd22710:
Pssm-ID: 469597 [Multi-domain] Cd Length: 94 Bit Score: 110.18 E-value: 1.38e-29
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain ...
162-416
7.17e-163
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 293298 Cd Length: 254 Bit Score: 458.15 E-value: 7.17e-163
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved ...
3-416
6.14e-64
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274166 [Multi-domain] Cd Length: 410 Bit Score: 210.76 E-value: 6.14e-64
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation ...
4-96
1.38e-29
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation protein D (YscD) and similar proteins; YscD protein is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD protein contains an N-terminal cytoplasmic domain, a transmembrane linker and a large periplasmic domain. The cytoplasmic domain consists of a forkhead-associated (FHA) fold. The FHA domain is a small phosphopeptide recognition module. Due to the lack of the conserved residues that are required for binding phosphothreonine, the cytoplasmic domain of YscD protein is therefore unlikely to function as a true FHA domain.
Pssm-ID: 438762 [Multi-domain] Cd Length: 94 Bit Score: 110.18 E-value: 1.38e-29
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
6-99
2.52e-29
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 109.66 E-value: 2.52e-29
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain ...
162-416
7.17e-163
Inner membrane component of T3SS, periplasmic domain; Yop-YscD-ppl is the periplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 293298 Cd Length: 254 Bit Score: 458.15 E-value: 7.17e-163
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved ...
3-416
6.14e-64
type III secretion apparatus protein, YscD/HrpQ family; This family represents a conserved protein of bacterial type III secretion systems. Gene symbols are variable from species to species. Members are designated YscD in Yersinia, HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this model describes the C-terminal 400 residues of a longer protein. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274166 [Multi-domain] Cd Length: 410 Bit Score: 210.76 E-value: 6.14e-64
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation ...
4-96
1.38e-29
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation protein D (YscD) and similar proteins; YscD protein is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD protein contains an N-terminal cytoplasmic domain, a transmembrane linker and a large periplasmic domain. The cytoplasmic domain consists of a forkhead-associated (FHA) fold. The FHA domain is a small phosphopeptide recognition module. Due to the lack of the conserved residues that are required for binding phosphothreonine, the cytoplasmic domain of YscD protein is therefore unlikely to function as a true FHA domain.
Pssm-ID: 438762 [Multi-domain] Cd Length: 94 Bit Score: 110.18 E-value: 1.38e-29
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
6-99
2.52e-29
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 109.66 E-value: 2.52e-29
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
4-81
1.90e-05
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 43.03 E-value: 1.90e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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