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Database: UniProt
Entry: A0A0D9YA42_9ORYZ
LinkDB: A0A0D9YA42_9ORYZ
Original site: A0A0D9YA42_9ORYZ 
ID   A0A0D9YA42_9ORYZ        Unreviewed;       763 AA.
AC   A0A0D9YA42;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OGLUM01G22000.2};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G22000.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM01G22000.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM01G22000.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   AlphaFoldDB; A0A0D9YA42; -.
DR   EnsemblPlants; OGLUM01G22000.2; OGLUM01G22000.2; OGLUM01G22000.
DR   Gramene; OGLUM01G22000.2; OGLUM01G22000.2; OGLUM01G22000.
DR   HOGENOM; CLU_000288_35_3_1; -.
DR   Proteomes; UP000026961; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002902; GNK2.
DR   InterPro; IPR038408; GNK2_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27002:SF76; OS10G0136400 PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51473; GNK2; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        370..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..217
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          233..340
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          443..731
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   763 AA;  83624 MW;  F22E7B90A6A5FD3A CRC64;
     MGKSSIEHGD EHGKQPRGDE HGSDCRVGQE QSEWSVRCNS KRALPDRQPR AALPAPAMAM
     PRRSVRRPRA PVSSAGLPPS QSHTHPVERI CMSSQASATG GASGTVPVLN PISMFCNSTA
     ARRTDPPNST FEANLASLVA AIVANASASG GFSAGSIGAA PDTVYGLALC RGDVTGADCA
     ACLSSTSVDY VQQWCGRSKE VTVYRDTCQL WFSDQDFVSA ASNIPETAAW NINNITEPVF
     PGWDPTTPRV FPSSLAPCIH YFLKQQTYST KKRFATAKTD IGGAFPTIYS LTQCTPDLSS
     ESCFKCLQGT IQESLKWFDG RRGGRIIGVR CLICFETSIF YNGEPMRIMG PSTNSTSADG
     NISKRKLSGL AVSIVFPVMG VLLFCVILGF GWIIRRNKIG KASLQEKTST YLYEEEALAW
     PIQGQSSELL FDFACIIRAT NNFSRENKIG EGGFGTIYKG KLDRLEIAVK RLDSHSGQGF
     VEFRNEIQLI AKLQHSNLVR LLGCCSKGEE KILVYEYLPN KSLDFFIFDE PNQRALLDWN
     KRLAIIEGIA QGLLYLHKHS RLRVTHRDLK ASNVLLDHNM DPKISDFGLA KIFSSNDIEG
     NTKRVAGTYG YMAPEYASEG LFSVKSDVFS FGVLTLEIVS GKRNPGFHQY GDFLNLLGYA
     WQLWTEGRWL KLIDVVLLTD CLVEAPLMMK CVNIALLCVQ ENAADRPTMS DVVAMLSSEG
     VSLPVPKHPA YFNVRVRNGE ASSAIDLELC SVNEVTITAP GCR
//
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