SpoIID/LytB domain-containing protein similar to Bacillus subtilis stage II sporulation protein D (spoIID) that may act at the level of sigma-G activity or its stability
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
199-537
2.73e-81
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 254.68 E-value: 2.73e-81
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
198-283
4.04e-33
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 121.55 E-value: 4.04e-33
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
199-537
2.73e-81
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 254.68 E-value: 2.73e-81
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the ...
200-538
2.49e-50
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the endospore formation program in a number of lineages in the Firmicutes (low-GC Gram-positive bacteria). It is expressed in the mother cell compartment, under control of Sigma-E. SpoIID, along with SpoIIM and SpoIIP, is one of three major proteins involved in engulfment of the forespore by the mother cell. [Cellular processes, Sporulation and germination]
Pssm-ID: 274332 [Multi-domain] Cd Length: 338 Bit Score: 176.06 E-value: 2.49e-50
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
198-283
4.04e-33
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 121.55 E-value: 4.04e-33
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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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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specific hits meet or exceed a domain-specific e-value threshold
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