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Database: UniProt
Entry: A0A199US25_ANACO
LinkDB: A0A199US25_ANACO
Original site: A0A199US25_ANACO 
ID   A0A199US25_ANACO        Unreviewed;      1038 AA.
AC   A0A199US25;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative LRR receptor-like serine/threonine-protein kinase {ECO:0000313|EMBL:OAY67608.1};
DE   Flags: Fragment;
GN   ORFNames=ACMD2_05224 {ECO:0000313|EMBL:OAY67608.1};
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY67608.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY67608.1, ECO:0000313|Proteomes:UP000092600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY67608.1};
RX   PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA   Redwan R.M., Saidin A., Kumar S.V.;
RT   "The draft genome of MD-2 pineapple using hybrid error correction of long
RT   reads.";
RL   DNA Res. 0:0-0(2016).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAY67608.1}.
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DR   EMBL; LSRQ01005443; OAY67608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199US25; -.
DR   STRING; 4615.A0A199US25; -.
DR   EnsemblPlants; Aco003845.1.mrna1; Aco003845.1.mrna1; Aco003845.1.path1.
DR   Gramene; Aco003845.1.mrna1; Aco003845.1.mrna1; Aco003845.1.path1.
DR   Proteomes; UP000092600; Unassembled WGS sequence.
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   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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF18; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00560; LRR_1; 5.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 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; PS51450; LRR; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAY67608.1};
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}; Receptor {ECO:0000313|EMBL:OAY67608.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        721..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          810..1038
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1038
FT                   /evidence="ECO:0000313|EMBL:OAY67608.1"
SQ   SEQUENCE   1038 AA;  110967 MW;  B23C016266EC5AFE CRC64;
     MSEEAATIPT LILLILSSIL ITGHVIEGLS DKVVIAQLKQ FLQEHNPINR GGYAEWDVSE
     PTPCNWSGIS CDGATKRVVG VDLSSSNISG PVFGNFSLLT ALARLDLSAN TIDGTLPADL
     NSCRGLRYLN ISHNLISGVL NVSGLANLEI LDVSLNRFEG PIAVNFPAGC ASLSVLNVST
     NKFTGEIAGV FDECEQLRYL DLSSNHFSGE IWQGFDSLRE FSVAENNLTG EILPGAFTAN
     CALETLDLSD NSISGAFPNS IANCSKLNFL SLSENGFGGA IPSGIGKLSE LESLFLGNNR
     FARDVPEELL NCSKLVFLDL NGNNFGGEVQ VIFGRFVTVK FLVLHGNNYT GGIEKSGILK
     LPEVSRLDLS FNSFSGPLPA SIAEMRKLKF LILAYNNFTG RIPAEYGNIA GLQALDLSFN
     ELSGEIPPSI GNLTSLLWLM LANNQLTGGI PPELGNCTSL LWVNLAGNRL AGVIPPEIAK
     MGRDPEPTFA TNREETGVAA GSGECLTMKR WLPANYPPFS FMYAVMTRKS CRTTWDRLLK
     GFGIIPVCLN TSSPVWTLAI SGYLQLSGNL LAGGVPPEIG GMRNLSLLHL DDNRLSGGLP
     REVGGIPLVS LNVSNNRFSG EIPSELGGIR CLEILDLSRN NFSGEFPASL NALAGLSKFN
     VSFNPRLSGV VSLTGQMATF YLNSFLGDPN ISFSSPAGGS PAQPPRGGGA AAASRRAARK
     VAFCVFVALT SAILTCGIIS FVLCLGVRTP VGPGPYPEEH LVKQRSHKAW SPASVSAAGS
     SSRPSDGIRV FRLDRTAFTY SDIVTATGNF SADLVIGRGG YGVVYRGVLP DGRHVAVKKL
     ERWGDDGGGE GEGEREFRAE MEVLAGRTGA GWPHPNLVPL YGWCLYGSAK LLVYEYMEGG
     CLESVIADWA LFGWEHRLET AVGVARALVF LHHECRPAVV HRDLKASNVL LDSRGTARVT
     DFGLARVVGP GETHVSTVVA GTVGYVAPEY GHTWQATTRG DVYSYGVLAM ELATGRRAVD
     GGEECLVEWG RRVGRDEA
//
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