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 ...
186-426
3.79e-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: 363.59 E-value: 3.79e-119
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The ...
535-695
5.17e-66
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: 218.19 E-value: 5.17e-66
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
186-426
3.79e-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: 363.59 E-value: 3.79e-119
FACT complex subunit (SPT16/CDC68); Proteins in this family are subunits the FACT complex. The ...
535-695
5.17e-66
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: 218.19 E-value: 5.17e-66
FACT complex subunit SPT16 N-terminal lobe domain; The FACT or facilitator of chromatin ...
11-172
9.62e-60
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: 200.85 E-value: 9.62e-60
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
188-417
2.15e-28
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: 113.49 E-value: 2.15e-28
Histone chaperone Rttp106-like; This family includes Rttp106, a histone chaperone involved in ...
819-895
7.38e-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: 93.26 E-value: 7.38e-23
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
186-420
3.18e-16
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: 78.26 E-value: 3.18e-16
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
186-420
1.14e-11
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: 65.22 E-value: 1.14e-11
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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