FACT complex subunit Spt16 (Supressor of Ty 16) family protein may be a component of the FACT (Facilitates Chromatin Transcription) complex, a histone chaperone comprising Spt16 and SSRP1, and which is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
180-420
6.84e-119
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.
Pssm-ID: 238524 [Multi-domain] Cd Length: 243 Bit Score: 364.75 E-value: 6.84e-119
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The ...
529-689
1.12e-74
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The FACT complex plays a role in transcription initiation and promotes binding of TATA-binding protein (TBP) to a TATA box in chromatin.
Pssm-ID: 462545 Cd Length: 151 Bit Score: 242.84 E-value: 1.12e-74
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
180-420
6.84e-119
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.
Pssm-ID: 238524 [Multi-domain] Cd Length: 243 Bit Score: 364.75 E-value: 6.84e-119
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The ...
529-689
1.12e-74
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The FACT complex plays a role in transcription initiation and promotes binding of TATA-binding protein (TBP) to a TATA box in chromatin.
Pssm-ID: 462545 Cd Length: 151 Bit Score: 242.84 E-value: 1.12e-74
FACT complex subunit SPT16 N-terminal lobe domain; The FACT or facilitator of chromatin ...
5-166
1.19e-59
FACT complex subunit SPT16 N-terminal lobe domain; The FACT or facilitator of chromatin transcription complex binds to and alters the properties of nucleosomes. This family represents the N-terminal lobe of the NTD, or N-terminal domain, and acts as a protein-protein interaction domain presumably with partners outside of the FACT complex. Knockout of the whole NTD domain, 1-450 residues in UniProt:P32558, in yeast serves to tender the cells sensitive to DNA replication stress but is not lethal. The C-terminal half of NTD is structurally similar to aminopeptidases, and the most highly conserved surface residues line a cleft equivalent to the aminopeptidase substrate-binding site, family peptidase_M24, pfam00557.
Pssm-ID: 464338 Cd Length: 160 Bit Score: 201.24 E-value: 1.19e-59
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
182-411
2.31e-27
Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.
Pssm-ID: 459852 [Multi-domain] Cd Length: 208 Bit Score: 110.79 E-value: 2.31e-27
Histone chaperone Rttp106-like; This family includes Rttp106, a histone chaperone involved in ...
813-889
4.70e-23
Histone chaperone Rttp106-like; This family includes Rttp106, a histone chaperone involved in heterochromatin-mediated silencing. This domain belongs to the Pleckstrin homology domain superfamily.
Pssm-ID: 462500 Cd Length: 84 Bit Score: 94.04 E-value: 4.70e-23
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
180-414
4.62e-15
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 75.18 E-value: 4.62e-15
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
180-414
2.70e-10
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.
Pssm-ID: 238525 [Multi-domain] Cd Length: 208 Bit Score: 60.99 E-value: 2.70e-10
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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Functional characterization of the conserved domain architecture found on the query.
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