uncharacterized protein Dmel_CG15734, isoform D [Drosophila melanogaster]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| MU2_FHA super family | cl39576 | Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain ... |
3-101 | 3.94e-10 | |||
Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain found in Drosophila mutator 2 (MU2) protein. FHA domains are generally phosphothreonine (pThr) specific-binding domains and are present in DNA repair and checkpoint proteins. However, phosphothreonine binding is not conserved in the MU2 active site pocket due to the absence of three key residues needed for pThr binding. Dimerization, is conserved between FHA domains of Drosophila MU2 and human MDC1 albeit through different interfaces. The MU2 FHA domain dimerizes via the beta-sheet 2, the MDC1 FHA domain dimerizes via the opposite beta-sheet 1. The actual alignment was detected with superfamily member pfam18221: Pssm-ID: 375648 Cd Length: 94 Bit Score: 52.10 E-value: 3.94e-10
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| Name | Accession | Description | Interval | E-value | |||
| MU2_FHA | pfam18221 | Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain ... |
3-101 | 3.94e-10 | |||
Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain found in Drosophila mutator 2 (MU2) protein. FHA domains are generally phosphothreonine (pThr) specific-binding domains and are present in DNA repair and checkpoint proteins. However, phosphothreonine binding is not conserved in the MU2 active site pocket due to the absence of three key residues needed for pThr binding. Dimerization, is conserved between FHA domains of Drosophila MU2 and human MDC1 albeit through different interfaces. The MU2 FHA domain dimerizes via the beta-sheet 2, the MDC1 FHA domain dimerizes via the opposite beta-sheet 1. Pssm-ID: 375648 Cd Length: 94 Bit Score: 52.10 E-value: 3.94e-10
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| FHA | cd00060 | forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
18-92 | 9.22e-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: 38.03 E-value: 9.22e-05
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| Name | Accession | Description | Interval | E-value | |||
| MU2_FHA | pfam18221 | Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain ... |
3-101 | 3.94e-10 | |||
Mutator 2 Fork head associated domain; This is the N-terminal forkhead-associated (FHA) domain found in Drosophila mutator 2 (MU2) protein. FHA domains are generally phosphothreonine (pThr) specific-binding domains and are present in DNA repair and checkpoint proteins. However, phosphothreonine binding is not conserved in the MU2 active site pocket due to the absence of three key residues needed for pThr binding. Dimerization, is conserved between FHA domains of Drosophila MU2 and human MDC1 albeit through different interfaces. The MU2 FHA domain dimerizes via the beta-sheet 2, the MDC1 FHA domain dimerizes via the opposite beta-sheet 1. Pssm-ID: 375648 Cd Length: 94 Bit Score: 52.10 E-value: 3.94e-10
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| FHA | cd00060 | forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
18-92 | 9.22e-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: 38.03 E-value: 9.22e-05
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| FHA_MDC1 | cd22665 | forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
36-99 | 8.08e-04 | |||
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module. Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 35.67 E-value: 8.08e-04
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| Blast search parameters | ||||
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