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Database: UniProt
Entry: K7LT62_SOYBN
LinkDB: K7LT62_SOYBN
Original site: K7LT62_SOYBN 
ID   K7LT62_SOYBN            Unreviewed;       946 AA.
AC   K7LT62;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=100797455 {ECO:0000313|EnsemblPlants:KRH24630};
GN   ORFNames=GLYMA_12G052300 {ECO:0000313|EMBL:KRH24630.1};
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:KRH24630.1};
RN   [1] {ECO:0000313|EMBL:KRH24630.1, ECO:0000313|EnsemblPlants:KRH24630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH24630};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH24630.1};
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:KRH24630}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH24630};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH24630.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH24630.1};
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00206}.
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DR   EMBL; CM000845; KRH24630.1; -; Genomic_DNA.
DR   RefSeq; XP_003540697.2; XM_003540649.3.
DR   AlphaFoldDB; K7LT62; -.
DR   SMR; K7LT62; -.
DR   STRING; 3847.K7LT62; -.
DR   PaxDb; 3847-GLYMA12G05630-2; -.
DR   EnsemblPlants; KRH24630; KRH24630; GLYMA_12G052300.
DR   GeneID; 100797455; -.
DR   Gramene; KRH24630; KRH24630; GLYMA_12G052300.
DR   KEGG; gmx:100797455; -.
DR   eggNOG; ENOG502QUN0; Eukaryota.
DR   HOGENOM; CLU_009948_1_0_1; -.
DR   InParanoid; K7LT62; -.
DR   OMA; TPAHFPF; -.
DR   OrthoDB; 1023652at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:UniProt.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   PANTHER; PTHR47460:SF3; RECEPTOR-LIKE KINASE; 1.
DR   PANTHER; PTHR47460; SERINE/THREONINE-PROTEIN KINASE-LIKE PROTEIN ACR4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF13540; RCC1_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00206};
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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          379..427
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          379..427
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          547..838
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          848..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        409..427
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
SQ   SEQUENCE   946 AA;  104190 MW;  51CE2F4C9E43B210 CRC64;
     MSKQFCYYYW SIFYILHFFL CVIFWLLCIM GFSLKHRLIY GFNVNQCSTR LLFELVILSH
     LWLQVTSLGS MSSIAISYGE KGSVFCGLKS DGSHTVTCYG SNSAIIYGTP THFSFLGLTA
     GDGFVCGLLM GSNQPYCWGS SAYIEMGVPQ PMIKGAQYLE ISAGDYHVCG LRKPMTGRHR
     NISLVDCWGY NMTKNYVFGA QIQSISAGSE FNCGLFSQNR TVFCWGDETN SLVISLIPHD
     MRFHKISAGG YHVCGISEGV SSKTFCWGRS LNLEEEISVS HAGQGNVDLA PNDPMLSVVG
     GKFHACGIKS YDRGVICWGF IIKPSTPSPK GIKVFEVAAG DYFTCAVLAV KSLMPSCWGV
     DFPTSLPLAV SPGMCQPAPC APGSYAIDQH KSLCKSPDSR VCMRCSGACP PEMHLKSACN
     LASDRVCEYN CSCCSSSECF LNCSSSYSNA AAAEKKSEKF WALQLPVLIA EIAFAVFVVS
     IVSITAVLYI RYRLRDCECS KGSMVKKLNG NSSLQNENKV RPDLEELKIR RAQTFTYEEL
     ETATSGFKEE SIVGKGSFSC VFKGVLKDGT VVAVKRAIVS PNMQKNSKEF HTELDLLSRL
     NHAHLLNLLG YCEEGGERLL VYEFMAHGSL HQHLHATNQV LREQLDWIRR VTIAVQAARG
     IEYLHGYACP PVIHRDIKSS NILIDEEHNA RVADFGLSLL GPADSGSPLA ELPAGTLGYL
     DPEYYRLHYL TTKSDVYSFG VLLLEILSGR KAIDMQYEEG NIVEWAVPLI KSGDITAILD
     PVLKPPPDLE ALKRIANVAC KCVRMRGKER PSMDKVTTAL ERGLAQLMGS PCIEQPILPT
     EVVLGSNRLH KKSSQRSSNR SVSETDVAET EDQRFEFRAP SWITFPSVTS SQRRKSSVSE
     ADVDGKNNAE GKNMGNVGGG GDVLRSLEEE IGPASPRERL FLQHNF
//
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