ID A5BZF6_VITVI Unreviewed; 978 AA.
AC A5BZF6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=VITISV_000471 {ECO:0000313|EMBL:CAN77413.1};
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:CAN77413.1};
RN [1] {ECO:0000313|EMBL:CAN77413.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(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; AM476757; CAN77413.1; -; Genomic_DNA.
DR ExpressionAtlas; A5BZF6; baseline and differential.
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 GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF23; RECEPTOR-LIKE PROTEIN KINASE HSL1; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..978
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002680091"
FT DOMAIN 647..953
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 978 AA; 108570 MW; 7EC0059B99AD6536 CRC64;
MALSCIFFLF VSLVXLSMPS QASITNQSHF FTLMKNSLSG BSLSDWDVTG KTSYCNYSGV
SCNDEGYVEV IDISGWSLSG RFPPDVCSYL PQLRVLRLSY NDLHDNFPEG IVNCSLLEEL
DMNGSQVIGT LPDLSPMKSL RILDLSYNLF TGEFPLSITN LTNLEHIRFN ENEGFNLWSL
PEDISRLTKL KSMILTTCMV HGQIPPSIGN MTSLVDLQLS GNFLNGQIPA ELGLLKNLRL
LELYYNQIAG RIPEELGNLT ELNDLDMSVN RLTGKIPESI CKLPKLRVLQ FYNNSLTGEI
PEAIGNSTAL AMLSIYDNFL TGGVPRSLGQ WSPMILLDLS ENHLSGELPT EVCKGGNLLY
FLVLDNMFSG KLPENYAKCE SLLRFRVSNN RLEGPIPEGL LGLPRVSILD LGFNNLNGQI
GKTIGTARNL SELFIQSNRI SGALPPEISQ ATNLVKIDLS NNLLSGPIPS EIGNLNKLNL
LLLQGNKFNS AIPKSLSSLK SVNVLDLSNN RLTGKIPESL SELLPNSINF TNNLLSGPIP
LSLIQGGLAE SFSGNPHLCV SVYVNSSDSN FPICSQXDNR KKLNCIWVIG ASSVIVIVGV
VLFLKRWFSK QRAVMEHDEN MSSSFFSYAV KSFHRINFBP REIIXALIDK NIVGHGGSGT
VYKIELSNGE VVAVKKLWSQ KTKDSASEDQ LFLVKELKTE VETLGSIRHK NIVKLYSCFS
SSDSSLLVYE YMPNGNLWDA LHRGRTLLDW PIRHRIALGI AQGLAYLHHD LLPPIIHRDI
KSTNILLEYQ LPTQSCRLRH SQVSCKQEGK ISLLLLLQGL MVTWPQHKLI LLVEPELLNS
FLLMVVTEYA YSSKATTKCD VYSFGVVLME LITGKKPVEA EFGENKNIIY WVATKVGTME
GAMEVLDKRL SGSFRDEMLQ MLRIGLRCTS SSPALRPTMN EVAQLLTEAD PCRVDSCKLS
CKTKETSNVT KTKNPFEL
//
