UniProt: F2DZF3

Database: UniProt
Entry: F2DZF3_HORVV

LinkDB:  F2DZF3_HORVV 
Original site:  F2DZF3_HORVV

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (4)   
   SMART (2)   
Literature (2)   
   PubMed (2)   
All databases (28)   

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ID   F2DZF3_HORVV            Unreviewed;      1104 AA.
AC   F2DZF3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509 {ECO:0000313|EMBL:BAK00475.1};
RN   [1] {ECO:0000313|EMBL:BAK00475.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21415278; DOI=10.1104/pp.110.171579;
RA   Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA   Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA   Sato K.;
RT   "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT   from 12 clone libraries.";
RL   Plant Physiol. 156:20-28(2011).
RN   [2] {ECO:0000313|Proteomes:UP000011116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   The International Barley Genome Sequencing Consortium;
RA   Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA   Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
RN   [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.6HG0627340.1}
RP   IDENTIFICATION.
RC   STRAIN=subsp. vulgare
RC   {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.6HG0627340.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2022) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; AK369273; BAK00475.1; -; mRNA.
DR   AlphaFoldDB; F2DZF3; -.
DR   STRING; 112509.F2DZF3; -.
DR   PaxDb; 4513-MLOC_10793-6; -.
DR   EnsemblPlants; HORVU.MOREX.r3.6HG0627340.1; HORVU.MOREX.r3.6HG0627340.1; HORVU.MOREX.r3.6HG0627340.
DR   Gramene; HORVU.MOREX.r2.6HG0520660.1; HORVU.MOREX.r2.6HG0520660.1; HORVU.MOREX.r2.6HG0520660.
DR   Gramene; HORVU.MOREX.r2.6HG0520660.1.mrna1; HORVU.MOREX.r2.6HG0520660.1.mrna1; HORVU.MOREX.r2.6HG0520660.1.
DR   Gramene; HORVU.MOREX.r3.6HG0627340.1; HORVU.MOREX.r3.6HG0627340.1; HORVU.MOREX.r3.6HG0627340.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   HOGENOM; CLU_000288_22_0_1; -.
DR   OrthoDB; 3681815at2759; -.
DR   Proteomes; UP000011116; Chromosome 6H.
DR   ExpressionAtlas; F2DZF3; baseline.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27008:SF514; OS02G0231700 PROTEIN; 1.
DR   PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 8.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000011116};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1104
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015090823"
FT   TRANSMEM        733..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          794..1100
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         823
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1104 AA;  118991 MW;  17DDE07B25B623B4 CRC64;
     MGWAVVLAIL ISSVLHPLLL TTLADESDNN RDALLCLKSR LSITTWNTTS PDFCSWRGVS
     CTRQPQLPVV VALDLEAQGL TGEIPPCMSN LTSLVRIHLP SNQLSGHLPP EIGRLTGLQY
     LNLSSNALSG EIPQSLSLCS SLEVVALRSN SIEGVIPLSL GTLRNLSSLD LSSNELSGEI
     PPLLGSSPAL ESVSLTNNFL NGEIPLFLAN CTSLRYLSLQ NNSLAGAIPA ALFNSLTITE
     IHISMNNLSG SIPLFTNFPS KLDYLDLTGN SLTGTVPPSV GNLTRLTGLL IAQNQLQGNI
     PDLSKLSDLQ FLDLSYNNLS GIVPPSIYNL PLLRFLGLAN NNLRGTLPSD MGNTLSNINS
     LIMSNNHFEG EIPASLANAS SMEFLYLGNN SLSGVVPSFG SMSNLQVVML HSNQLEAGDW
     TFLSSLANCT ELQKLNLGGN KLSGNLPAGS VATLPKRMNG LTLQSNYISG TIPLEIGNLS
     EISLLYLDNN LFTGPIPSTL GQLSNLFILD LSWNKFSGEI PPSMGNLNQL TEFYLQENEL
     TGSIPTSLAG CKKLVALNLS SNGLNGSING PMFSKLYQLS WLLDISHNQF RDSIPPEIGS
     LINLGSLNLS HNKLTGKIPS TLGACVRLES LNLGGNHLEG SIPQSLANLK GVKALDFSQN
     NLSGTIPKFL ETFTSLQYLN MSFNNFEGPV PIGGVFDNTS GVSFQGNALL CSNAQVNDLP
     RCSTSASQRK RKFIVPLLAA LSAVVALALI LGLVFLVFHI LRKKRERSSQ SIDHTYTEFK
     RLTYNDVSKA TNGFSPTNIV GSGQFGIVYK GQLDGKDSSV AVKVFKLNQY GALDSFIAEC
     KALRNIRHRN LVSVITACST YDLMGNEFKA LVFQYMANGS LENRLHAKLQ NNADLSLGTV
     ICIAVDIASA LEYLHNQCTP PVVHCDLKPS NILFDDDDTS YVCDFGLARL IHGYSSEAQS
     SSTSIAGPGG TIGYIAPEYG MGSQISTEGD VYSYGIILLE MLTGKRPTDE TFGNGLTLQK
     YVDASLSEIE RVLRPSLMPK IGDQPTITPK IEEYRATTVM HICALQLVKL GLLCSVESPK
     DRPSMHEIYS EVIAVKEAFF SMNS
//

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