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Database: UniProt
Entry: F6I4B8_VITVI
LinkDB: F6I4B8_VITVI
Original site: F6I4B8_VITVI 
ID   F6I4B8_VITVI            Unreviewed;       926 AA.
AC   F6I4B8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   OrderedLocusNames=VIT_05s0062g01440 {ECO:0000313|EMBL:CCB61833.1};
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:CCB61833.1, 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).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; FN596745; CCB61833.1; -; Genomic_DNA.
DR   RefSeq; XP_002268601.2; XM_002268565.4.
DR   AlphaFoldDB; F6I4B8; -.
DR   STRING; 29760.F6I4B8; -.
DR   PaxDb; 29760-VIT_05s0062g01440-t01; -.
DR   EnsemblPlants; Vitvi05g01376_t001; Vitvi05g01376_P001; Vitvi05g01376.
DR   GeneID; 100253795; -.
DR   Gramene; Vitvi05g01376_t001; Vitvi05g01376_P001; Vitvi05g01376.
DR   KEGG; vvi:100253795; -.
DR   eggNOG; ENOG502QPQ4; Eukaryota.
DR   HOGENOM; CLU_000288_114_6_1; -.
DR   InParanoid; F6I4B8; -.
DR   OrthoDB; 1029940at2759; -.
DR   Proteomes; UP000009183; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR   PANTHER; PTHR47986:SF10; RECEPTOR-LIKE KINASE TMK4; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF08263; LRRNT_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
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   3: Inferred from homology;
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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..926
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003338098"
FT   TRANSMEM        487..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          581..861
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          442..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   926 AA;  99652 MW;  DCCFCF6A7B883D73 CRC64;
     MEDSSTPMLL LTFTCLCLSL SANTTTADEA AFMTKLAAAL SPTPSGWSGT NHCKWSGVKC
     DAIGQVISIN LASRSLSGML PSDINQLPQL QALSLQKNQL SGPLPSLSNL TSLQSVFLDN
     NNFSSVPPEF LLGLNSLQTF SISENPSLQP WRIPEHLSES TSLASLLASN ANIFGTIPEI
     FGSFPNLQSV RLSYNNLTGP LPPSFGGSGI QNLWLNNQKV GLSGRLDVLG AMVQLSQAWL
     HANAFSGPIP DLSNSSAIFD LQLRDNQLTG VLLPSLFSHP RLVNISLQNN KLQGPYPNFS
     KTVEVTLGST NNFCNPQPGP CDPQVTALLE VAKALGYPMI LAQSWEGNDA CKGWSFISCD
     AQGKNVTIVN FGKQEWSGSI SPAFANLTSL RNLLLNDNDL SGTLPASLTS LKELRILDIS
     NNNLSGSLPH FPSTVSVKAQ GNNLLGTNST SAGDGGASGS GSPASNSDST PTTTPSKATS
     SSSSPGFLVS VIVGSAVFMG IVSLVIYGLY AKRRHRKLVM SKRSLKGKGS VRSLITGKAN
     GNGTSGSDSH NQSSSSGDMH VYDGGNVAIP IEVLRQVTNN FDEANILGKG GFGVVYRGEL
     HDGTQIAVKR MESAIVGTKG LSEFQAEIGV LTKVRHRHLV ALLGFCINGN ERLLVYEYMP
     QGTLGQHLFE YNETGFSPLT WKQRITIALD VAKGMEYLHS LAQQSFIHRD LKPSNILLGT
     DMRAKVSDFG LVKNAPDGKY SVETRLAGTF GYLAPEYAAT GRVTIKVDVF AFGVVLMEMI
     TGRKSLDEAL PEEKSHLVSW FRRVLPNPDN IRDALDPSLH PDEETFRSIC EVAELAGHCT
     AREPHQRPDM SHAVNVLSHL LDEWKPSADD EENDNFGIDD FNLSLPQALE RWQANEGTSS
     MTLNLYNSGA QSISKKRSAS HSLDQQ
//
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