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Q84P25 (4CLL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-coumarate--CoA ligase-like 2

EC=6.2.1.-
Gene names
Name:4CLL2
Ordered Locus Names:At1g20480
ORF Names:F5M15.29
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentPeroxisome
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5655654-coumarate--CoA ligase-like 2
PRO_0000299175

Regions

Nucleotide binding221 – 2299ATP By similarity
Nucleotide binding360 – 3656ATP By similarity
Region288 – 35972SBD1 By similarity
Region360 – 42465SBD2 By similarity
Motif563 – 5653Microbody targeting signal Potential

Sites

Binding site4451ATP By similarity
Binding site4601ATP By similarity
Binding site5511ATP By similarity

Experimental info

Sequence conflict131E → V in AAP03016. Ref.1
Sequence conflict741R → Q in AAP03016. Ref.1
Sequence conflict1821S → T in AAP03016. Ref.1
Sequence conflict3551V → F in AAP03016. Ref.1
Sequence conflict5051M → V in AAP03016. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q84P25 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 0226F2C09AA3031B

FASTA56561,438
        10         20         30         40         50         60 
MAVKHGVDGD GSEIESRTLA VDRKSGFCES TSIFYSKREP MALPPNQFLD VTSFIASQPH 

        70         80         90        100        110        120 
RGKTVFVDAV TGRRLSFPEL WLGVERVAGC LYALGVRKGN VVIILSPNSI LFPIVSLSVM 

       130        140        150        160        170        180 
SLGAIITTAN PINTSDEISK QIGDSRPVLA FTTCKLVSKL AAASNFNLPV VLMDDYHVPS 

       190        200        210        220        230        240 
QSYGDRVKLV GRLETMIETE PSESRVKQRV NQDDTAALLY SSGTTGTSKG VMLSHRNLIA 

       250        260        270        280        290        300 
LVQAYRARFG LEQRTICTIP MCHIFGFGGF ATGLIALGWT IVVLPKFDMA KLLSAVETHR 

       310        320        330        340        350        360 
SSYLSLVPPI VVAMVNGANE INSKYDLSSL HTVVAGGAPL SREVTEKFVE NYPKVKILQG 

       370        380        390        400        410        420 
YGLTESTAIA ASMFNKEETK RYGASGLLAP NVEGKIVDPD TGRVLGVNQT GELWIRSPTV 

       430        440        450        460        470        480 
MKGYFKNKEA TASTIDSEGW LKTGDLCYID GDGFVFVVDR LKELIKCNGY QVAPAELEAL 

       490        500        510        520        530        540 
LLAHPEIADA AVIPIPDMKA GQYPMAYIVR KVGSNLSESE IMGFVAKQVS PYKKIRKVTF 

       550        560 
LASIPKNPSG KILRRELTKL TTSKL 

« Hide

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. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY250833 mRNA. Translation: AAP03016.1.
AC027665 Genomic DNA. Translation: AAF79612.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29977.1.
IPIIPI00518444.
PIRD86338.
RefSeqNP_173472.1. NM_101898.3.
UniGeneAt.41707.
At.69772.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ84P25.
SMRQ84P25. Positions 33-559.
ModBaseSearch...

Protein-protein interaction databases

IntActQ84P25. 1 interaction.
STRINGQ84P25.

Proteomic databases

PRIDEQ84P25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G20480.1; AT1G20480.1; AT1G20480.
GeneID838636.
GenomeReviewsGene locus AT1G20480 in contig CT485782_GR.
KEGGath:AT1G20480.
NMPDRfig|3702.1.peg.2394.

Organism-specific databases

TAIRAt1g20480.

Phylogenomic databases

eggNOGKOG1176.
GeneTreeEPGT00070000028073.
HOGENOMHBG547964.
InParanoidQ84P25.
OMASAVETHR.
PhylomeDBQ84P25.
ProtClustDBCLSN2679410.

Gene expression databases

ArrayExpressQ84P25.
GenevestigatorQ84P25.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name4CLL2_ARATH
AccessionPrimary (citable) accession number: Q84P25
Secondary accession number(s): Q9LMV7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families