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Database: UniProt
Entry: D7MAP5_ARALL
LinkDB: D7MAP5_ARALL
Original site: D7MAP5_ARALL 
ID   D7MAP5_ARALL            Unreviewed;       766 AA.
AC   D7MAP5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=ARALYDRAFT_912621 {ECO:0000313|EMBL:EFH43220.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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DR   EMBL; GL348719; EFH43220.1; -; Genomic_DNA.
DR   RefSeq; XP_002866961.1; XM_002866915.1.
DR   AlphaFoldDB; D7MAP5; -.
DR   STRING; 81972.D7MAP5; -.
DR   EnsemblPlants; scaffold_700363.1; scaffold_700363.1; scaffold_700363.1.
DR   GeneID; 9303033; -.
DR   Gramene; scaffold_700363.1; scaffold_700363.1; scaffold_700363.1.
DR   KEGG; aly:9303033; -.
DR   eggNOG; ENOG502QRF8; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   OrthoDB; 470880at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR   PANTHER; PTHR48010:SF29; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 5.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..766
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003103487"
FT   TRANSMEM        330..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          447..754
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          303..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  83912 MW;  7576B328CB7CF54E CRC64;
     MKMELISVVF FFFFCSVLSS SGLNSDGLVL MKFKSSVLVD PLSLLQTWNY KHETPCSWRG
     ISCNNDSKVL TLSLPNSQLL GSIPSDLGSL LTLKSLDLSN NSFNGPLPVS FFNARELRFL
     DLSSNMISGE IPSAIGDLHN LLTLNLSDNA LAGKLPANLA SLRNLTVVSL ENNYFSGEIP
     GGWRVVEFLD LSSNLINGSL PPDFGGDSLR YLNVSFNQIS GEIPPEIGVN FPRNVTVDLS
     FNNLTGPIPD SPVFFNQESN FFSGNPGLCG EPTRNPCLIP SSPSIASNAD VPTSTPAIAA
     IPNTIGSNPV TDPKSQQTDP NARTGLRPGV IIGIVVGDIA GIGILAVIFL YIYRCKKNKI
     VDNNNDKQRT ETDTITLSPF TSSSSSPEES RRFKKWSCLR KDPETTPSEE DNDEDEESGY
     NANQRSGDNK LVTVDGEKEM EIETLLKASA YILGATGSSI MYKAVLEDGR VFAVRRLGEN
     GLNQRRFKDF ESHIRAIGKL VHPNLVRLCG FYWGTDEKLV IYDFVPNGSL VNPRYRKGGG
     SSSPYHLPWE TRLKIAKGIA RGLSYLHEKK HVHGNLKPSN ILLGHDMEPK ISDFGLERLL
     TGETSYIRAG GSSRIFSSKR YTTSSREFSS MGPTPSPSPS SVGPMSPYCA PESFRSLKPS
     PKWDVYGFGV ILLELLTGKI VSVEEIVLGN GLTVEDRHRA VRMADVAIRG ELDGKQEFLL
     DCFKLGYSCA SPVPQKRPTM KESLAVLERF HPNSSVIKSS SFHYGH
//
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