Q84P24 (4CLL6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-coumarate--CoA ligase-like 6
EC=6.2.1.-

Alternative name(s):
4-coumarate--CoA ligase isoform 7
Short name=At4CL7

Gene names

Name:	4CLL6
Ordered Locus Names:	At4g19010
ORF Names:	F13C5.180

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
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.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred 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 – 566	566	4-coumarate--CoA ligase-like 6		PRO_0000299179
Regions
	Nucleotide binding	212 – 220	9	ATP By similarity
	Nucleotide binding	357 – 362	6	ATP By similarity
	Region	286 – 356	71	SBD1 By similarity
	Region	357 – 421	65	SBD2 By similarity
	Motif	564 – 566	3	Microbody targeting signal Potential
Sites
	Binding site	442	1	ATP By similarity
	Binding site	457	1	ATP By similarity
	Binding site	548	1	ATP By similarity
Experimental info
	Sequence conflict	89	1	I → T in BAC42032. Ref.5
	Sequence conflict	89	1	I → T in AAO64847. Ref.6
	Sequence conflict	170	1	S → P in AAP03017. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q84P24 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: A4EE22717B17E349	FASTA	566	61,957
	10 20 30 40 50 60 MAATHLHIPP NPKTQTSHQN PPFWFSSKTG IYTSKFPSLH LPVDPNLDAV SALFSHKHHG 70 80 90 100 110 120 DTALIDSLTG FSISHTELQI MVQSMAAGIY HVLGVRQGDV VSLVLPNSVY FPMIFLSLIS 130 140 150 160 170 180 LGAIVTTMNP SSSLGEIKKQ VSECSVGLAF TSTENVEKLS SLGVSVISVS ESYDFDSIRI 190 200 210 220 230 240 ENPKFYSIMK ESFGFVPKPL IKQDDVAAIM YSSGTTGASK GVLLTHRNLI ASMELFVRFE 250 260 270 280 290 300 ASQYEYPGSS NVYLAALPLC HIYGLSLFVM GLLSLGSTIV VMKRFDASDV VNVIERFKIT 310 320 330 340 350 360 HFPVVPPMLM ALTKKAKGVC GEVFKSLKQV SSGAAPLSRK FIEDFLQTLP HVDLIQGYGM 370 380 390 400 410 420 TESTAVGTRG FNSEKLSRYS SVGLLAPNMQ AKVVDWSSGS FLPPGNRGEL WIQGPGVMKG 430 440 450 460 470 480 YLNNPKATQM SIVEDSWLRT GDIAYFDEDG YLFIVDRIKE IIKYKGFQIA PADLEAVLVS 490 500 510 520 530 540 HPLIIDAAVT AAPNEECGEI PVAFVVRRQE TTLSEEDVIS YVASQVAPYR KVRKVVMVNS 550 560 IPKSPTGKIL RKELKRILTN SVSSRL

References

	« Hide 'large scale' referencesShow '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]	"Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase genes." Lawrence P.K. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"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	AY250834 mRNA. Translation: AAP03017.1. AY376733 mRNA. Translation: AAQ86592.1. AL021711 Genomic DNA. Translation: CAA16758.1. AL161549 Genomic DNA. Translation: CAB78903.1. CP002687 Genomic DNA. Translation: AEE84125.1. AK117362 mRNA. Translation: BAC42032.1. BT005912 mRNA. Translation: AAO64847.1.
IPI	IPI00532784.
PIR	F85214. T05038.
RefSeq	NP_193636.1. NM_118019.2.
UniGene	At.43659.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q84P24.
SMR	Q84P24. Positions 47-543.
ModBase	Search...
Proteomic databases
PRIDE	Q84P24.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G19010.1; AT4G19010.1; AT4G19010.
GeneID	827639.
GenomeReviews	Gene locus AT4G19010 in contig CT486007_GR.
KEGG	ath:AT4G19010.
NMPDR	fig|3702.1.peg.19713.
Organism-specific databases
TAIR	At4g19010.
Phylogenomic databases
eggNOG	KOG1176.
GeneTree	EPGT00070000028073.
HOGENOM	HBG547964.
InParanoid	Q84P24.
OMA	EASQYEY.
PhylomeDB	Q84P24.
ProtClustDB	PLN02574.
Gene expression databases
Genevestigator	Q84P24.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. 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

4CLL6_ARATH

Accession

Primary (citable) accession number: Q84P24
Secondary accession number(s): O49414, Q8GYV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	September 21, 2011
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program