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Database: UniProt
Entry: F6HY74_VITVI
LinkDB: F6HY74_VITVI
Original site: F6HY74_VITVI 
ID   F6HY74_VITVI            Unreviewed;       782 AA.
AC   F6HY74;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   OrderedLocusNames=VIT_09s0002g03120 {ECO:0000313|EMBL:CCB59397.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB59397.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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DR   EMBL; FN596494; CCB59397.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HY74; -.
DR   STRING; 29760.F6HY74; -.
DR   PaxDb; 29760-VIT_09s0002g03120-t01; -.
DR   eggNOG; ENOG502QQCZ; Eukaryota.
DR   HOGENOM; CLU_000288_41_1_1; -.
DR   InParanoid; F6HY74; -.
DR   Proteomes; UP000009183; Chromosome 9.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45631:SF196; LRR RECEPTOR-LIKE SERINE_THREONINE-KINASE; 1.
DR   PANTHER; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
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:UP000009183};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   TRANSMEM        430..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          482..750
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   782 AA;  86487 MW;  BD99FC134F37E4E1 CRC64;
     MDVRSFPEGD RNCYALPPGQ GKNHKYLIRA WFMYGNYDSK NQPLVFKLYL GVDEWATVNI
     TNASVIIRKE IIHIPTTDDI DVCLVNAGSG TPFISVLELQ QLNDSIYSPT EPGSLLLHDR
     WDFGTQKEKS KDDVYDRIWR PFTKSSWESI NSSVVRSSFS VSDYKLPGIV MATAATPANE
     SEPLRISLDI DDDPSQKLYI YMHFAEVKEG VFREFTTFVN DDEAWGGTVL TTYLFSYTAE
     SDYSMSGSTT KKLSFSLKRT NRSTLPPIIN AMEVYIIKEF SQASTQQNDV DAIKGIKSEY
     AVSRNWQGDP CLPIKYQWDG LTCSLDISPA IITLNLSSSN LAGNILTSFS GLKSLQNLDL
     SYNNLTGPVP EFFADLPSLT TLNLTGNNLT GSVPQAVMDK LKDGTLSLGE NPSLCQSASC
     QGKEKKKSRF LVPVLIAIPN VIVILILITA LAMIIRKFRR RETKEKSGNS EFTYSEVVSI
     TNNFSQTIGR GGFGQVFLGT LADGTQVAVK VHSESSIQEA KALQAEVKLL TRVHHKNLVR
     LIGYCDDGTN MVLIYEYMSN GNLQQKLSGR EAADVLNWEE RLQIAVDAAH GLEYLHNGCK
     PPIVHRDMKS SNILLTETLE AKIADFGMSR DLESGALLST DPVGTPGYLD PEYQSAGLNK
     KSDVYSFGIV LLELLTGRPA IIPGGIYIVV WVSHMIERGD IESIVDRRLQ GEFNTNSAWK
     AVEIALACVA STGMQRPDMS HVVVDLKECL ETGVASRRIK MVGSHLEDVP VVLSTESAPH
     AR
//
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