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Database: UniProt
Entry: A0A1E5UPJ3_9POAL
LinkDB: A0A1E5UPJ3_9POAL
Original site: A0A1E5UPJ3_9POAL 
ID   A0A1E5UPJ3_9POAL        Unreviewed;       984 AA.
AC   A0A1E5UPJ3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Receptor protein kinase TMK1 {ECO:0000313|EMBL:OEL14783.1};
GN   ORFNames=BAE44_0024198 {ECO:0000313|EMBL:OEL14783.1};
OS   Dichanthelium oligosanthes.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX   NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL14783.1, ECO:0000313|Proteomes:UP000095767};
RN   [1] {ECO:0000313|EMBL:OEL14783.1, ECO:0000313|Proteomes:UP000095767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OEL14783.1};
RA   Studer A.J., Schnable J.C., Brutnell T.P.;
RT   "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT   species.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OEL14783.1}.
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DR   EMBL; LWDX02069002; OEL14783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5UPJ3; -.
DR   STRING; 888268.A0A1E5UPJ3; -.
DR   OrthoDB; 1210136at2759; -.
DR   Proteomes; UP000095767; 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: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; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR   PANTHER; PTHR47986:SF1; RECEPTOR-LIKE KINASE TMK2; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OEL14783.1};
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}; Receptor {ECO:0000313|EMBL:OEL14783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095767};
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};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..984
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009187248"
FT   DOMAIN          617..910
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          469..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   984 AA;  104838 MW;  BC05A151A826F675 CRC64;
     MPSPTARRRR REGAAGLWCA PVLLALVALA AGAAAQTAPS DVAAMRAVAK ALGADKALGW
     DVAGDPCSPK PWDRVSCDSS GRVIAIQVGG YSLTGTLAPE VRNLTALTRL EVFGNFLSGP
     LPSLAGLSSL QVLLARDNNF TSIPADFFKG LTELVAVDID HNQLAPWMLP DDLATCTSLT
     NFSANNVSIT GTLPDFFGAM PGLQRLSLAY NQLSGPVPAS LAGAPLVQLW LNNQQNGNRF
     NGSISFVSNM TALEQLWLQS NAFTGPLPDF TGFVSLSDLQ LRDNQLTGPV PDSLVTLVKS
     KALKKLTLTN NLLQGPMPQF SGEGNGKPDG VDLMATTERF CLQDPGKPCD PRVSLLLEVA
     AGFLYPMTLA DDWKGNDPCN GFTTVTCDTK GNIIALNFGR KGLSGSIPPA IGKIGSLQRL
     ILSNNNITGT VPEEVAAMPN LTEVDLSNNN LYGKLPTFTS KSAVVKTAGN PNIGKDAPAP
     TAGSGGTSNN SPSGGGSSGG IGNNEGSSSS SVGVIAGSVV GAVAGLGLVA ALGFYCYKRK
     QKPFGRVQSP HAMVIHPRHS GSDDMVKITV AGGNVNGGAR ASETYSQASS GPRDIHVVES
     GNMVISIQVL RNVTNNFSED NILGRGGFGT VYKGELHDGT KIAVKRMEAG VMGNKGLNEF
     KSEIAVLTKV RHRNLVSLLG YCADGNERIL VYEYMPQGTL SQHLFEWSEN NLRPLEWKKR
     LSIALDVARG VEYLHSLAQQ TFIHRDLKPS NILLGDDMKA KVADFGLVRL APTDGKCVSV
     ETRLAGTFGY LAPEYAGDHP ISLLLKYIVT GRVTTKADVF SFGVILMELI TGRKALDETQ
     PEDSMHLVTW FRRMQLNKDT FRKAIDPVID LDEETFASVS TVSELAGHCC AREPHQRPDM
     GHAVNVLSTL SDVWKPTDPD SDDSYGIDLD MTLPQALKKW QAFEDSSHFD GATSSFVASL
     DNTQTSIPTR PPGFAESFTS ADGR
//
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