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Database: UniProt
Entry: A0A0E0M493_ORYPU
LinkDB: A0A0E0M493_ORYPU
Original site: A0A0E0M493_ORYPU 
ID   A0A0E0M493_ORYPU        Unreviewed;       945 AA.
AC   A0A0E0M493;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC09G17280.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC09G17280.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC09G17280.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   -!- 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A0E0M493; -.
DR   STRING; 4537.A0A0E0M493; -.
DR   EnsemblPlants; OPUNC09G17280.1; OPUNC09G17280.1; OPUNC09G17280.
DR   Gramene; OPUNC09G17280.1; OPUNC09G17280.1; OPUNC09G17280.
DR   eggNOG; ENOG502SGW3; Eukaryota.
DR   HOGENOM; CLU_000288_116_4_1; -.
DR   OMA; FTYVIIS; -.
DR   Proteomes; UP000026962; Chromosome 9.
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   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   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF237; OS09G0551150 PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 3.
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; PS50948; PAN; 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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..945
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002367103"
FT   DOMAIN          26..151
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          335..422
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          492..770
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         519
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   945 AA;  104757 MW;  76FA123DC48CEDA0 CRC64;
     MDQSAAFTYV IISVVVLLLP PPCSSDDRLV PGKPLTSDAT VVSDGGAFAM GFFSPSNSTP
     AKLYLGIWYN DIPVRTVVWV ANQETPVTNG TTLSLTDSSN LVVSDADGRV HWTTNITGGA
     AGNGNTTAVL INTGNLVVRS PNGTVLWQSF EHPTDSFLPG MKLRMTYRTR ASDRLVSWRG
     PGDPSPGSFS YGGDPATFLQ MIMWNGTRPV MRDGPWTGYM VDSQYQTNTS AIVYLAIIDT
     DEEIYITFSV ADDAPHTRFV LTYAGKYQLQ RWSSGSSAWV VLQEWPTGCD PYDFCGPNGY
     CDNTAAEALP TCRCLEGFEP ASAAEWSSGR FSRGCRRTEA VQCSDRMKPP DKFVHVANRT
     MEACAAECSG SCSCVAYAYA NLSSSRSRGD TTRCLVWSGE LIDTGKVGLG SGDSDTLYLR
     LAGLDTGGTT KSDAIKIVLP VLASKRRNRQ KHRELILDVT STSDEVGKGN LAQDFEFLSV
     KFEDIALATH NFSEAYKIGE GGFGKVYKAM IGGQEVAVKR LSRDSQQGTE EFRNEVILIA
     KLQHRNLVRL LGCCVERDEK LLIYEYLPNK SLDATLFDGS RKLKLDWTVR FNIIKGVARG
     LLYLHQDSRL TIIHRDLKAS NVLLDAEMRP KIADFGMARI FCDNQQNANT RRVVGTYGYM
     APEYAMEGIF STKSDVYSFG VLLLEVITGI RRSSTSNIMD FPNLIIYAWN MWKEGKTKDL
     ADSSIIDSCS LDEVLLCIHV ALLCVQENPN DRPLMSSTVF ILENGSSTAL PAPSRPAYFA
     YRSDESEQSR ENIQNSMNTF TLTNIEGRPK IAADFGMARI FCDSQQNANT RSVVRTYNHA
     NEMIEQYAMK AWNMWKEGNT EDLADSSIID SCLLDERPLM SSTVFILENG SSTALPAPNH
     PAYFAYRSDE LEQSRENIQN SMNTFTLANI EGWTFKKYLR LNFNH
//
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