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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//