Reviewed,
UniProtKB/Swiss-Prot Q84P25 (4CLL2_ARATH)
Last modified
June 16, 2009.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 4-coumarate--CoA ligase-like 2 EC=6.2.1.- | ||||||
| Gene names |
| ||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 565 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Subcellular location | Peroxisome Potential. |
| Domain | Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity By similarity. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
| Sequence caution | The sequence AAF79612.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 3 genes: At1g20480, At1g20490 and At1g20500. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Peroxisome |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 565 | 565 | 4-coumarate--CoA ligase-like 2 | PRO_0000299175 | |||||
Regions | |||||||||
| Nucleotide binding | 221 – 229 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 360 – 365 | 6 | ATP By similarity | ||||||
| Region | 288 – 359 | 72 | SBD1 By similarity | ||||||
| Region | 360 – 424 | 65 | SBD2 By similarity | ||||||
| Motif | 563 – 565 | 3 | Microbody targeting signal Potential | ||||||
Sites | |||||||||
| Binding site | 445 | 1 | ATP By similarity | ||||||
| Binding site | 460 | 1 | ATP By similarity | ||||||
| Binding site | 551 | 1 | ATP By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 13 | 1 | E → V in AAP03016. Ref.1 | ||||||
| Sequence conflict | 74 | 1 | R → Q in AAP03016. Ref.1 | ||||||
| Sequence conflict | 182 | 1 | S → T in AAP03016. Ref.1 | ||||||
| Sequence conflict | 355 | 1 | V → F in AAP03016. Ref.1 | ||||||
| Sequence conflict | 505 | 1 | M → V in AAP03016. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases." Shockey J.M., Fulda M.S., Browse J. Plant Physiol. 132:1065-1076(2003) [PubMed: 12805634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION. Strain: cv. Wassilewskija. |
| [2] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | "The substrate specificity-determining amino acid code of 4-coumarate:CoA ligase." Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D., Kombrink E., Stuible H.-P. Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003) [PubMed: 12819348] [Abstract] Cited for: GENE FAMILY ORGANIZATION. |
Cross-references
Sequence databases | |
|---|---|
| AY250833 mRNA. Translation: AAP03016.1. AC027665 Genomic DNA. Translation: AAF79612.1. Sequence problems. | |
| IPI | IPI00518444. |
| PIR | D86338. |
| RefSeq | NP_173472.1. |
| UniGene | At.41707 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LCI based on UniProtKB P08659. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q84P25. |
Genome annotation databases | |
| GeneID | 838636. |
| GenomeReviews | Gene locus AT1G20480 in contig CT485782_GR. |
| KEGG | ath:AT1G20480. |
| NMPDR | fig|3702.1.peg.2394. |
Organism-specific databases | |
| TAIR | At1g20480. |
Phylogenomic databases | |
| OMA | Q84P25. SAVETHR. |
Gene expression databases | |
| ArrayExpress | Q84P25. |
Family and domain databases | |
| InterPro | IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | 4CLL2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q84P25 Secondary accession number(s): Q9LMV7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


