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Database: UniProt
Entry: A0A199UQT2_ANACO
LinkDB: A0A199UQT2_ANACO
Original site: A0A199UQT2_ANACO 
ID   A0A199UQT2_ANACO        Unreviewed;       870 AA.
AC   A0A199UQT2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   ORFNames=ACMD2_13996 {ECO:0000313|EMBL:OAY67158.1};
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:OAY67158.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY67158.1, 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:OAY67158.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433,
CC         ECO:0000256|PIRNR:PIRNR000641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC         ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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:OAY67158.1}.
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DR   EMBL; LSRQ01005643; OAY67158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199UQT2; -.
DR   STRING; 4615.A0A199UQT2; -.
DR   EnsemblPlants; Aco002680.1.mrna1; Aco002680.1.mrna1.cds1; Aco002680.1.path1.
DR   Gramene; Aco002680.1.mrna1; Aco002680.1.mrna1.cds1; Aco002680.1.path1.
DR   Proteomes; UP000092600; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0048544; P:recognition of pollen; IEA:InterPro.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47974:SF27; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 2.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 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|PIRNR:PIRNR000641};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Lectin {ECO:0000313|EMBL:OAY67158.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:OAY67158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..870
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008508096"
FT   TRANSMEM        456..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..167
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          545..811
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          712..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   870 AA;  92664 MW;  6EED521DEC109F7D CRC64;
     MSPSSSSSSS SSSLFKLSSF LLLLLLCFRF FYVADATTKV AVEFIYPNFS ASALLFFDTY
     GVFLASGSSA FQAAVFNPPN QQSRYYLAVL HAASKTVVWA ANRAAPIPDN SGLVLLSTLG
     LSITSSNGSL LWSTPTLRSS VAALRLLDSG NLLLVNAANA TLWQSFDHPS DSLLSSQLVP
     TGSYLTSYVS DNDFAEGDYR LVVTTSDAVL TWLGSRYWSL AGDVRSIKDD DDAVAFMTAN
     YTGLSLLSSV GGVVIKVYLP AAELRIVKLG SDGRLQITSY SSLNSSSPSS SKFVAPSGPC
     DLPLSCGTFN LCTPKGNSPS CNCLPLFAPS PNGGCLPGDG SVLASSSSCG SNDLSKSSSS
     YLSLRSGTVY FENKFAAPVS SGRDEPTCRG ICTGNCSCIG YFFDGSSKSC YILEHQMGSF
     LNSTASEAAD TLGYIKIVGT ASPPNTPSSN SPTTHLVAIL LPSIAAFLLI FMLALIMLVW
     WRKRIKKRMK RFKTMVMKEI QLGRHKSPGR ASSDFDYDDD DAGEEILIPG MPTRFTYEEL
     EVVTGNFRTK IGSGGFGSVY KGELPDKSPV AVKKIEGVGF QGRREFCTEI AVIGNIRHVN
     LVRLRGFCAQ GARRLLVYEF MNRGSLDRPL FGSGAGPVLE WGERMAVAVG AARGLAYLHS
     ECDHKIVHCD VKPENILLAD GGQVKIADFG LAKLMGPDQS GLFTTMRGRA RAVSDGESGG
     GRAGRGSTGG GCGGGGGGGE YFPLLALERH EQGRYQELAD PRLEGRVVEE EVRRVVKVAL
     CCLHEEPALR PSMAAMVGML EGKAEASEPR VESLGFLRLY GRGYVDPASN EGMDAAAHKG
     FFTGGDTTGS VMSTTTAQSY VSSQEVSGPR
//
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