strawberry notch (SBNO) family protein similar to Drosophila melanogaster protein strawberry notch that is a Notch pathway component and may contribute to the specificity between lateral and inductive Notch signaling pathways in the wing disk
C-terminal domain on Strawberry notch homolog; Strawberry notch proteins carry DExD/H-box groups upstream of this domain. The function of this domain is not known. These proteins promote the expression of diverse targets, potentially through interactions with transcriptional activator or repressor complexes.
:
Pssm-ID: 464009 Cd Length: 269 Bit Score: 497.85 E-value: 3.11e-166
C-terminal domain on Strawberry notch homolog; Strawberry notch proteins carry DExD/H-box groups upstream of this domain. The function of this domain is not known. These proteins promote the expression of diverse targets, potentially through interactions with transcriptional activator or repressor complexes.
Pssm-ID: 464009 Cd Length: 269 Bit Score: 497.85 E-value: 3.11e-166
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
323-476
3.22e-05
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 45.47 E-value: 3.22e-05
C-terminal domain on Strawberry notch homolog; Strawberry notch proteins carry DExD/H-box groups upstream of this domain. The function of this domain is not known. These proteins promote the expression of diverse targets, potentially through interactions with transcriptional activator or repressor complexes.
Pssm-ID: 464009 Cd Length: 269 Bit Score: 497.85 E-value: 3.11e-166
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
323-476
3.22e-05
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 45.47 E-value: 3.22e-05
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
323-440
1.54e-03
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 40.62 E-value: 1.54e-03
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
293-438
4.53e-03
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 39.21 E-value: 4.53e-03
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
901-984
5.71e-03
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 37.96 E-value: 5.71e-03
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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