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Database: UniProt
Entry: A0A3L6QDQ7_PANMI
LinkDB: A0A3L6QDQ7_PANMI
Original site: A0A3L6QDQ7_PANMI 
ID   A0A3L6QDQ7_PANMI        Unreviewed;       990 AA.
AC   A0A3L6QDQ7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Receptor-like protein kinase HSL1 {ECO:0000313|EMBL:RLM78794.1};
GN   ORFNames=C2845_PM12G07350 {ECO:0000313|EMBL:RLM78794.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM78794.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
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:RLM78794.1}.
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DR   EMBL; PQIB02000012; RLM78794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6QDQ7; -.
DR   STRING; 4540.A0A3L6QDQ7; -.
DR   Proteomes; UP000275267; Chromosome 12.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd14066; STKc_IRAK; 1.
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; 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; PTHR45974:SF272; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE FLS2; 1.
DR   PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR   Pfam; PF00560; LRR_1; 7.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
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; 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:RLM78794.1};
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:RLM78794.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..990
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018165760"
FT   TRANSMEM        596..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          649..930
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          952..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         680
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   990 AA;  107324 MW;  8BDF78D769CF17FD CRC64;
     MAHSYLLLLL FLLMFLTSIS SLRSMAQLAT DQETLLTIKK DWGSPPALSS WNPQNASSHC
     SWAGVSCGKN GQSLSYLDLS YNNLTNQFPT AFYGCSALQY LDLSNNHFSD GAPHLSCNGF
     TGSVPLAIAA FSKLKSLVLD TNSFNGTYPS SAIAKLSELE TLTLASNPFA PGPIPDEFSK
     LTNLKILWLS GMNLTGGIPD GLSSLTELTT LALYDNKLDG GIPSWVWKLQ KLELLYLYEN
     SFTGGIGPEV TAFSLQQLDL SSNWLTGRMP EAIGEMKNLK MLYLYYNNLT GPIPASIGLL
     PNLVDIRPFN NRLFGPLPPE LGKHSLLGNL EVSNNLLNGT VPDTLSLNKK LYDIVLFNNE
     FSGELPAALG ACDTLDNIML QNNHLAGEFP EEVWSAFPKL TTVKIQNNNF TGTLPSVISS
     NITRIEMGNN LFSGEVPSSA PGLKSFMAEN NRFSGELPAN MSGFANLTDL NLAGNQISGS
     IPPSIRSLGR LNYLNLSSNL ISGGIPAEIG LLPVLTMFDL SNNELTGKIP EELTNLGLHL
     SSLNLSSNQL TGELPESLQS PAFDEAFLGN LGLCTTVNLN MNIPACYRGH NQMSTGLIIL
     FSVVAGVILI GAVGCFIIRR KTRGRDLTTW KVTPFRKVDF TENDILSKLR EENVIGSGGS
     GKVYRVHLGG RVGAVVAVKK LWSRGKAEEK LDKEFDSEVR ILGDIRHNNI VSLLCYMSSE
     DTKLLVYEYM ENGSLDRWLH PRDPAGAGAT APLDWPTRLG IAIDAARDLS YMHHESAQPI
     MHRDVKSSNI LLDPGFRAKI ADFGLARILV KSGEPESVSA VGGTFGYMAP ECGRGVKVNQ
     KVDVYSFGVV LLELATGRVA NDDGAECCLV EWAWRRYKAG GPLHDVVDGG IRDRAVHAKD
     AVAVFLLRVM CTGDDATSRP SMKQVLQQLL QYDRTSSVAG ACRDGGDDDI ARAQLPKGRK
     GEQGAKRPLD SGGEFWDGDE ESGGFVAHPV
//
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