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9CAUD:D9ZNF3
Contents
Species (Taxon ID) | Clostridium phage phiCTP1. (871584) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Endolysin (ECO:0000313 with EMBL:ADL40330.1) | |
External Links | ||
UniProt | D9ZNF3 | |
EMBL | HM159959 | |
RefSeq | YP_003856822.1 | |
PDB | 4CU2 5A6S | |
PDBsum | 4CU2 5A6S | |
ProteinModelPortal | D9ZNF3 | |
SMR | D9ZNF3 | |
CAZy | GH25 | |
GeneID | 9711352 | |
KEGG | vg:9711352 | |
Proteomes | UP000002251 | |
GO | GO:0003796 GO:0005975 GO:0016998 GO:0009253 | |
Gene3D | 3.20.20.80 | |
InterPro | IPR002053 IPR013781 IPR017853 | |
Pfam | PF01183 | |
SUPFAM | SSF51445 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000315 |
P |
In figure 4 they show a sequence alignment on the nucleotide level of CTP1L and CS74L. In the figure there are other related endolysins shown that are present. The putative Shine-Dalgarno region is shown in figure 4a and 4b in the red. It also indicates that the start codon is GTG. The nucleotide sequence used during E. coli expression of when they did the sequence alignment was derived from the original bacteriophage DNA. To test whether the wild-type sequence encoded a secondary translation site to the wild type. |
complete | |||||
enables |
GO:0003796 |
lysozyme activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0016998 |
cell wall macromolecule catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Dunne, M et al. (2016) Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J. Biol. Chem. 291 4882-93 PubMed GONUTS page