Reviewed, UniProtKB/Swiss-Prot Q9SZ67 (WRK19_ARATH)

Names and origin

Protein names

Recommended name:
    Probable WRKY transcription factor 19
Alternative name(s):
    WRKY DNA-binding protein 19

Gene names

Name:	WRKY19
Ordered Locus Names:	At4g12020
ORF Names:	F16J13.90

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	1895 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. May act also as a disease resistance protein with a serine/threonine-protein kinase activity By similarity.
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the disease resistance X-TIR-NB-LRR-X family. Contains 7 LRR (leucine-rich) repeats. Contains 1 NB-ARC domain. Contains 1 PAH (paired amphipathic helix) repeat. Contains 1 protein kinase domain. Contains 2 WRKY DNA-binding domains.

Ontologies

Keywords
Biological process	Plant defense Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: InterPro innate immune response Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR intrinsic to membrane Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from electronic annotation. Source: InterPro transmembrane receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SZ67-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1895	1895	Probable WRKY transcription factor 19		PRO_0000133661
Regions
	Repeat	323 – 369	47	PAH
	Domain	800 – 1087	288	NB-ARC
	Repeat	1204 – 1226	23	LRR 1
	Repeat	1257 – 1281	25	LRR 2
	Repeat	1304 – 1327	24	LRR 3
	Repeat	1328 – 1348	21	LRR 4
	Repeat	1349 – 1371	23	LRR 5
	Repeat	1372 – 1395	24	LRR 6
	Repeat	1419 – 1443	25	LRR 7
	Domain	1626 – 1877	252	Protein kinase
	DNA binding	462 – 526	65	WRKY 1
	DNA binding	635 – 700	66	WRKY 2
	Nucleotide binding	844 – 851	8	ATP Potential
	Nucleotide binding	1632 – 1640	9	ATP By similarity
	Compositional bias	35 – 39	5	Poly-Ser
	Compositional bias	87 – 90	4	Poly-Ser
	Compositional bias	97 – 307	211	Gly-rich
	Compositional bias	980 – 983	4	Poly-Leu
	Compositional bias	1568 – 1571	4	Poly-Ser
Sites
	Active site	1758	1	By similarity
	Binding site	1654	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1C19D3EE164C9363	FASTA	1,895	210,322
	10 20 30 40 50 60 MSEKEELPLT LTSIGAATAT SDYHQRVGSS GEGISSSSSD VDPRFMQNSP TGLMISQSSS 70 80 90 100 110 120 MCTVPPGMAA TPPISSGSGL SQQLNNSSSS KLCQVEGCQK GARDASGRCI SHGGGRRCQK 130 140 150 160 170 180 PDCQKGAEGK TVYCKAHGGG RRCEYLGCTK GAEGSTDFCI AHGGGRRCNH EDCTRSAWGR 190 200 210 220 230 240 TEFCVKHGGG ARCKTYGCGK SASGPLPFCR AHGGGKKCSH EDCTGFARGR SGLCLMHGGG 250 260 270 280 290 300 KRCQRENCTK SAEGLSGLCI SHGGGRRCQS IGCTKGAKGS KMFCKACITK RPLTIDGGGN 310 320 330 340 350 360 MGGVTTGDAL NYLKAVKDKF EDSEKYDTFL EVLNDCKHQG VDTSGVIARL KDLFKGHDDL 370 380 390 400 410 420 LLGFNTYLSK EYQITILPED DFPIDFLDKV EGPYEMTYQQ AQTVQANANM QPQTEYPSSS 430 440 450 460 470 480 AVQSFSSGQP QIPTSAPDSS LLAKSNTSGI TIIEHMSQQP LNVDKQVNDG YNWQKYGQKK 490 500 510 520 530 540 VKGSKFPLSY YKCTYLGCPS KRKVERSLDG QVAEIVYKDR HNHEPPNQGK DGSTTYLSGS 550 560 570 580 590 600 STHINCMSSE LTASQFSSNK TKIEQQEAAS LATTIEYMSE ASDNEEDSNG ETSEGEKDED 610 620 630 640 650 660 EPEPKRRITE VQVSELADAS DRTVREPRVI FQTTSEVDNL DDGYRWRKYG QKVVKGNPYP 670 680 690 700 710 720 RFSSSKDYDV VIRYGRADIS NEDFISHLRA SLCRRGISVY EKFNEVDALP KCRVLIIVLT 730 740 750 760 770 780 STYVPSNLLN ILEHQHTEDR VVYPIFYRLS PYDFVCNSKN YERFYLQDEP KKWQAALKEI 790 800 810 820 830 840 TQMPGYTLTD KSESELIDEI VRDALKVLCS ADKVNMIGMD MQVEEILSLL CIESLDVRSI 850 860 870 880 890 900 GIWGTVGIGK TTIAEEIFRK ISVQYETCVV LKDLHKEVEV KGHDAVRENF LSEVLEVEPH 910 920 930 940 950 960 VIRISDIKTS FLRSRLQRKR ILVILDDVND YRDVDTFLGT LNYFGPGSRI IMTSRNRRVF 970 980 990 1000 1010 1020 VLCKIDHVYE VKPLDIPKSL LLLDRGTCQI VLSPEVYKTL SLELVKFSNG NPQVLQFLSS 1030 1040 1050 1060 1070 1080 IDREWNKLSQ EVKTTSPIYI PGIFEKSCCG LDDNERGIFL DIACFFNRID KDNVAMLLDG 1090 1100 1110 1120 1130 1140 CGFSAHVGFR GLVDKSLLTI SQHNLVDMLS FIQATGREIV RQESADRPGD RSRLWNADYI 1150 1160 1170 1180 1190 1200 RHVFINDTGT SAIEGIFLDM LNLKFDANPN VFEKMCNLRL LKLYCSKAEE KHGVSFPQGL 1210 1220 1230 1240 1250 1260 EYLPSKLRLL HWEYYPLSSL PKSFNPENLV ELNLPSSCAK KLWKGKKARF CTTNSSLEKL 1270 1280 1290 1300 1310 1320 KKMRLSYSDQ LTKIPRLSSA TNLEHIDLEG CNSLLSLSQS ISYLKKLVFL NLKGCSKLEN 1330 1340 1350 1360 1370 1380 IPSMVDLESL EVLNLSGCSK LGNFPEISPN VKELYMGGTM IQEIPSSIKN LVLLEKLDLE 1390 1400 1410 1420 1430 1440 NSRHLKNLPT SIYKLKHLET LNLSGCISLE RFPDSSRRMK CLRFLDLSRT DIKELPSSIS 1450 1460 1470 1480 1490 1500 YLTALDELLF VDSRRNSPVV TNPNANSTEL MPSESSKLEI LGTPADNEVV VGGTVEKTRG 1510 1520 1530 1540 1550 1560 IERTPTILVK SREYLIPDDV VAVGGDIKGL RPPVLQLQPA MKLSHIPRGS TWDFVTHFAP 1570 1580 1590 1600 1610 1620 PETVAPPSSS SEAREEEVET EETGAMFIPL GDKETCSFTV NKGDSSRTIS NTSPIYASEG 1630 1640 1650 1660 1670 1680 SFITCWQKGQ LLGRGSLGSV YEGISADGDF FAFKEVSLLD QGSQAHEWIQ QVEGGIALLS 1690 1700 1710 1720 1730 1740 QLQHQNIVRY RGTTKDESNL YIFLELVTQG SLRKLYQRNQ LGDSVVSLYT RQILDGLKYL 1750 1760 1770 1780 1790 1800 HDKGFIHRNI KCANVLVDAN GTVKLADFGL AKVMSLWRTP YWNWMAPEVI LNPKDYDGYG 1810 1820 1830 1840 1850 1860 TPADIWSLGC TVLEMLTGQI PYSDLEIGTA LYNIGTGKLP KIPDILSLDA RDFILTCLKV 1870 1880 1890 NPEERPTAAE LLNHPFVNMP LPSSGSGSVS SLLRG

References

[1]

"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.

Web resources

NIB-LRRS

Functional and comparative genomics of disease resistance gene homologs

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL049638 Genomic DNA. Translation: CAB40943.1. AL161533 Genomic DNA. Translation: CAB78245.1.
IPI	IPI00519247.
PIR	T06609.
RefSeq	NP_001118968.1.
UniGene	At.3076
3D structure databases
HSSP	HSSP built from PDB template 1F3M based on UniProtKB Q13153.
ModBase	Search...
Proteomic databases
PRIDE	Q9SZ67.
Genome annotation databases
GeneID	826810.
GenomeReviews	Gene locus AT4G12020 in contig CT486007_GR.
KEGG	ath:AT4G12020.
Organism-specific databases
GeneFarm	1664. 89.
TAIR	At4g12020.
Gene expression databases
ArrayExpress	Q9SZ67.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR006210. EGF-like. IPR001611. Leu-rich_rpt. IPR011713. Leu-rich_rpt_3. IPR002182. NB-ARC. IPR003822. PAH. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. IPR003657. WRKY_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.20.1160.11. PAH. 1 hit.
Pfam	PF00560. LRR_1. 2 hits. PF07725. LRR_3. 1 hit. PF00931. NB-ARC. 1 hit. PF02671. PAH. 1 hit. PF00069. Pkinase. 1 hit. PF03106. WRKY. 2 hits. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00382. AAA. 1 hit. SM00181. EGF. 1 hit. SM00220. S_TKc. 1 hit. SM00774. WRKY. 2 hits. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS50811. WRKY. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

WRK19_ARATH

Accession

Primary (citable) accession number: Q9SZ67

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)