ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q06548


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name APK1A_ARATH
Primary accession number Q06548
Secondary accession number Q9LNY0
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name Protein kinase APK1A, chloroplastic [Precursor]
Synonym EC 2.7.11.1
Gene name
Name: APK1A
OrderedLocusNames: At1g07570
ORFNames: F22G5.5
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1007/BF00046450; PubMed=1450380 [NCBI, ExPASy, EBI, Israel, Japan]
Hirayama T., Oka A.;
"Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine.";
Plant Mol. Biol. 20:653-662(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D12522; BAA02092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC022464; AAF79545.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004055; AAO42086.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT005112; AAO50645.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S28615; S28615.
RefSeq NP_172237.1; -.
NP_973778.1; -.
UniGene At.348
3D structure databases
ModBase Q06548.
Organism-specific databases
GeneFarm 1710; 129.
TAIR At1g07570; -.
Gene expression databases
ArrayExpress Q06548; -.
GermOnline AT1G07570; Arabidopsis thaliana.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q06548.
Genome annotation databases
GeneID 837271; -.
GenomeReviews CT485782_GR; AT1G07570.
KEGG ath:AT1G07570; -.
NMPDR fig|3702.1.peg.941; -.
Other
ProtoNet Q06548.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Chloroplast; Complete proteome; Kinase; Nucleotide-binding; Plastid; Serine/threonine-protein kinase; Transferase; Transit peptide; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    38  38     Chloroplast (Potential). 
CHAIN   39   410  372     Protein kinase APK1A, chloroplastic. PRO_0000024302
DOMAIN   68   352  285     Protein kinase. 
NP_BIND   74    82  9     ATP (By similarity). 
ACT_SITE   203   203        Proton acceptor (By similarity). 
BINDING   106   106        ATP (By similarity). 
Sequence information
Length: 410 AA [This is the length of the unprocessed precursor] Molecular weight: 45519 Da [This is the MW of the unprocessed precursor] CRC64: 5BAB28D9E0065082 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGICLSAQVK AESSGASTKY DAKDIGSLGS KASSVSVRPS PRTEGEILQS PNLKSFSFAE 

        70         80         90        100        110        120 
LKSATRNFRP DSVLGEGGFG CVFKGWIDEK SLTASRPGTG LVIAVKKLNQ DGWQGHQEWL 

       130        140        150        160        170        180 
AEVNYLGQFS HRHLVKLIGY CLEDEHRLLV YEFMPRGSLE NHLFRRGLYF QPLSWKLRLK 

       190        200        210        220        230        240 
VALGAAKGLA FLHSSETRVI YRDFKTSNIL LDSEYNAKLS DFGLAKDGPI GDKSHVSTRV 

       250        260        270        280        290        300 
MGTHGYAAPE YLATGHLTTK SDVYSFGVVL LELLSGRRAV DKNRPSGERN LVEWAKPYLV 

       310        320        330        340        350        360 
NKRKIFRVID NRLQDQYSME EACKVATLSL RCLTTEIKLR PNMSEVVSHL EHIQSLNAAI 

       370        380        390        400        410 
GGNMDKTDRR MRRRSDSVVS KKVNAGFARQ TAVGSTVVAY PRPSASPLYV 

Q06548 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!