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Database: UniProt
Entry: A0A0R0EN05_SOYBN
LinkDB: A0A0R0EN05_SOYBN
Original site: A0A0R0EN05_SOYBN 
ID   A0A0R0EN05_SOYBN        Unreviewed;       531 AA.
AC   A0A0R0EN05;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRG91188.1, ECO:0000313|EnsemblPlants:KRG91188};
GN   Name=100789002 {ECO:0000313|EnsemblPlants:KRG91188};
GN   ORFNames=GLYMA_20G139000 {ECO:0000313|EMBL:KRG91188.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG91188.1};
RN   [1] {ECO:0000313|EMBL:KRG91188.1, ECO:0000313|EnsemblPlants:KRG91188}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG91188};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG91188.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG91188}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG91188};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG91188.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG91188.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; CM000853; KRG91188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0EN05; -.
DR   EnsemblPlants; KRG91188; KRG91188; GLYMA_20G139000.
DR   Gramene; KRG91188; KRG91188; GLYMA_20G139000.
DR   Proteomes; UP000008827; Chromosome 20.
DR   ExpressionAtlas; A0A0R0EN05; baseline and differential.
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   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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27002:SF510; CYSTEINE-RICH RECEPTOR-KINASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF00069; Pkinase; 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:UP000008827};
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|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..531
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014520816"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..132
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          138..257
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          354..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   531 AA;  60316 MW;  18C69D5C11C488C9 CRC64;
     MALIPSMMLF SFLSFLVILK SEANNDQLQF VYHYCNNEYG NITTETYSDN RNNLLSNMYY
     DKENDYGFYN SSYGQDPDKV YAIGFCRGDA NLDKCRSCLE KSAVLLRERC PVQKEGIGWF
     DECMLRYTNH SIFGVMVTQP NNIMCNTKNA PKDPRSAAGF DQVVHNLLNE LRNRTTTVAD
     PESDSSRSRK FFAEGDAPVQ SSNVTIHALI QCTPDISSQN CTRCLEHAMT NILYCDGKRG
     GRYLGPSCSV RYEIYPFFEP IVHHAPPPQP ATQVTTTTGK EKSNPSRTII AIVVPVVAVV
     VLLVAFTYNY LGARRRRQKP FQSEGGEGEL DNDIKIDELL QFDFATIKFA TNNFSDANKL
     GQGGFGIVYK GTLSDGQEIA IKRLSINSNQ GETEFKNEIL LTGKLQHRNL VRLLGFCFSR
     RERLLIYEFV PNKSLDYFIF DPNNRVNLNW ERRYNIIRGI ARGLLYLHED SRLQVVHRDL
     KTSNILLDEE LNPKISDFGM ARLFEINQTQ ASTNTIVGTF FQSSQMSLVL A
//
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