ID F6I583_VITVI Unreviewed; 1022 AA.
AC F6I583;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN OrderedLocusNames=VIT_19s0015g01120 {ECO:0000313|EMBL:CCB62038.1};
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:CCB62038.1, 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; FN596747; CCB62038.1; -; Genomic_DNA.
DR AlphaFoldDB; F6I583; -.
DR STRING; 29760.F6I583; -.
DR PaxDb; 29760-VIT_19s0015g01120-t01; -.
DR eggNOG; ENOG502QSU9; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; F6I583; -.
DR Proteomes; UP000009183; Chromosome 19.
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: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; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF24; PROTEIN KINASE DOMAIN-CONTAINING 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; 9.
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; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 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 644..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 698..976
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 727
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1022 AA; 111040 MW; 74A75A8F06F35AA8 CRC64;
MPATLRNLLL SPNIFSFSFT FLLSINSLFF SCCFSIDEQG QALLTWKNGL NSSTDVLRSW
NPSDPSPCNW FGVHCNPNGE VVQISLRSVD LQGPLPSNFQ SLNSLKSLIL PSANLTGTIP
KEFGEYRELA LIDLSGNSIT GEIPEEICRL SKLQSLSLNT NFLEGEIPSN IGNLSSLVYL
TLYDNQLSGE IPKSIGELTK LEVFRAGGNQ NLKGELPWEI GNCTNLVMIG LAETSISGSL
PLSIGMLKRI QTIAIYTALL SGPIPQEIGN CSELQNLYLY QNSISGPIPR GIGELAKLRS
LLLWQNSFVG TIPSEIGACS ELTVIDLSEN LLSGSIPGSF GNLLKLRELQ LSVNQLSGFI
PSEITNCTAL NHLEVDNNDI SGEIPVLIGN LKSLTLLFAW QNKLTGSIPE SLSNCENLQA
LDLSYNHLSG SIPKQIFGLK NLTKFLDLHS NGLISSVPDT LPISLQLVDV SDNMLTGPLT
PYIGSLVELT KLNLGKNRLS GTIPAEILSC SKLQLLDLGN NGFSGEIPKE LGQLPALEIS
LNLSCNQLTG EIPSQFSSLS KLGVLDLSHN KLTGNLNILT SLQNLVFLNV SYNDFSGELP
DTPFFRNLPM SDLAGNRALY ISNGVVARAD SIGRGGHTKS AMKLAMSILV SASAVLVLLA
IYMLVRARVA NRLLENDTWD MTLYQKLDFS IDDIIRNLTS ANVIGTGSSG VVYRVAIPDG
QTLAVKKMWS SEESGAFSSE IRTLGSIRHR NIVRLLGWGS NRSLKLLFYD YLPNGSLSSL
LHGAGKGGAD WEARYDVVLD VAHAVAYLHH DCVPAILHGD VKAMNVLLGP KLEAYLADFG
LARVVNNSGE DDFSKMGQRP HLAGSYGYMA PEHASMQRIT EKSDVYSFGV VLLEVLTGRH
PLDPTLPGGA HLVQWVRDHL SKKLDPVDIL DPKLRGRADP QMHEMLQTLA VSFLCISTRA
EDRPMMKDVV AMLKEIRQVD ALRAETDLLK GDLSTLPSSP PTHNMVLQGS SNCSFAFSDE
SV
//
