B2FU16 (B2FU16_STRMK) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 30.
History...
Names and origin
| Protein names | Submitted name: Putative ATP-dependent DNA ligase EMBL CAQ43668.1 | ||
| Gene names |
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| Organism | Stenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP] EMBL CAQ43668.1 | ||
| Taxonomic identifier | 522373 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group › ![]() |
Protein attributes
| Sequence length | 828 AA. |
| Sequence status | Complete. |
| Protein existence | Predicted |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Ligase EMBL CAQ43668.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA recombination Inferred from electronic annotation. Source: InterPro DNA repairInferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activityInferred from electronic annotation. Source: InterPro DNA primase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants." Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. Avison M.B.Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K279a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM743169 Genomic DNA. Translation: CAQ43668.1. |
| RefSeq | YP_001969984.1. NC_010943.1. |
3D structure databases | |
| ProteinModelPortal | B2FU16. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 522373.Smlt0053. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAQ43668; CAQ43668; Smlt0053. |
| GeneID | 6391857. |
| KEGG | sml:Smlt0053. |
| PATRIC | 23695853. VBISteMal45202_0046. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3285. |
| HOGENOM | HOG000222509. |
| KO | K01971. |
| OMA | LVAECEF. |
| ProtClustDB | CLSK299585. |
Enzyme and pathway databases | |
| BioCyc | SMAL522373:GJE8-50-MONOMER. |
Family and domain databases | |
| Gene3D | 2.40.50.140. 1 hit. |
| InterPro | IPR012309. DNA_ligase_ATP-dep_C. IPR012310. DNA_ligase_ATP-dep_cent. IPR014146. DNA_pol_LigD_ligase_dom. IPR002755. DNA_primase_S. IPR014144. LigD_PE_domain. IPR014145. LigD_pol. IPR012340. NA-bd_OB-fold. IPR014143. NHEJ_ligase_prk. [Graphical view] |
| Pfam | PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF01896. DNA_primase_S. 1 hit. PF13298. LigD_N. 1 hit. [Graphical view] |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. |
| TIGRFAMs | TIGR02777. LigD_PE_dom. 1 hit. TIGR02778. ligD_pol. 1 hit. TIGR02779. NHEJ_ligase_lig. 1 hit. TIGR02776. NHEJ_ligase_prk. 1 hit. |
| PROSITE | PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | B2FU16_STRMK | ||||||||
| Accession | Primary (citable) accession number: B2FU16 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with

