Q9SU91 (Q9SU91_ARATH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
UDP-N-acetylglucosamine O-acyltransferase domain-containing protein EMBL AEE85642.1

Submitted name:
UDP-N-acetylglucosamine O-acyltransferase-like protein EMBL CAB45314.1

Gene names

Name:	T16L4.50 EMBL CAB45314.1
Synonyms:	AT4g29540 EMBL CAB79712.1
Ordered Locus Names:	At4g29540 TAIR At4g29540 EMBL BAD43226.1
ORF Names:	AT4G29540 EMBL AEE85642.1

Organism

Arabidopsis thaliana (Mouse-ear cress) EMBL CAB45314.1

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	336 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Molecular function	Acyltransferase EMBL CAB45314.1 Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	transferase activity, transferring acyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9SU91 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D51A40A3FAED226A	FASTA	336	36,714
	10 20 30 40 50 60 MISLLKAREK LLSPLVSSTI RRLSSSLSYS REDSRDSEVL IHPSAVVHPN AVIGKGVSVG 70 80 90 100 110 120 PYCTIGSSVK LGNGCKLYPS SHVFGNTELG ESCVLMTGAV VGDELPGYTF IGCNNIIGHH 130 140 150 160 170 180 AVVGVKCQDL KYKHGDECFL CIGNNNEIRE FCSIHRSSKP SDKTVIGDNN LIMGSCHIAH 190 200 210 220 230 240 DCKIGDRNIF ANNTLLAGHV VVEDNTHTAG ASVVHQFCHI GSFAFIGGGS VVSQDVPKYM 250 260 270 280 290 300 MVAGERAELR GLNLEGLRRN GFTMSEMKSL RAAYRKIFMS TETVSLSFEE RLTELEQDQE 310 320 330 LYSVPAVSAM LQSIRDSFTE SRRGICKFRQ WLDSTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." EU, CSHL and WU Arabidopsis Sequencing Project 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.
[2]	EU Arabidopsis sequencing project Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	EU Arabidopsis sequencing project Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	Bevan M., Rose M., Hempel S., Entian K.-D., Bancroft I., Mewes H.W., Mayer K.F.X., Lemcke K., Schueller C. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[7]	Rose M., Hempel S., Entian K.-D., Mewes H.W., Lemcke K., Mayer K.F.X. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002687 Genomic DNA. Translation: AEE85642.1. AK175463 mRNA. Translation: BAD43226.1. AL079344 Genomic DNA. Translation: CAB45314.1. AL161575 Genomic DNA. Translation: CAB79712.1.
IPI	IPI00657302.
PIR	T09917.
RefSeq	NP_001031749.1. NM_001036672.1.
UniGene	At.31911.
3D structure databases
HSSP	HSSP built from PDB template 1LXA based on UniProtKB P10440.
ProteinModelPortal	Q9SU91.
SMR	Q9SU91. Positions 34-327.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SU91.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G29540.2; AT4G29540.2; AT4G29540.
GeneID	829075.
KEGG	ath:AT4G29540.
Organism-specific databases
TAIR	At4g29540.
Phylogenomic databases
GeneTree	EPGT00050000016891.
OMA	REFCTFN.
PhylomeDB	Q9SU91.
ProtClustDB	CLSN2680157.
Gene expression databases
Genevestigator	Q9SU91.
Family and domain databases
InterPro	IPR001451. Hexapep_transf. IPR011004. Trimer_LpxA-like. [Graphical view]
KO	K00677.
Pfam	PF00132. Hexapep. 4 hits. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 2 hits.
ProtoNet	Search...

Entry information

Entry name

Q9SU91_ARATH

Accession

Primary (citable) accession number: Q9SU91

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)