ID A0A072V841_MEDTR Unreviewed; 1027 AA.
AC A0A072V841;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=MTR_2g040910 {ECO:0000313|EMBL:KEH37523.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH37523.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH37523.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH37523.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH37523,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH37523.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH37523.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH37523,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH37523}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH37523};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM001218; KEH37523.1; -; Genomic_DNA.
DR RefSeq; XP_013463488.1; XM_013608034.1.
DR AlphaFoldDB; A0A072V841; -.
DR EnsemblPlants; KEH37523; KEH37523; MTR_2g040910.
DR Gramene; KEH37523; KEH37523; MTR_2g040910.
DR HOGENOM; CLU_000288_22_0_1; -.
DR Proteomes; UP000002051; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0099402; P:plant organ development; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008:SF523; LRR RECEPTOR-LIKE KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KEH37523.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:KEH37523.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 660..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 715..1022
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1027 AA; 114033 MW; D41E7FFBE8FF43DB CRC64;
MKSFSLLSPP LLYLHLLFLL TFNLMWFGPN KIRAVAAIGN QTDHLALLKF KESISSDPYK
ALESWNSSIH FCKWHGITCS PMHERVTELS LKRYQLHGSL SPHVCNLTFL KTLDIGDNNF
FGEIPQELGQ LLHLQQLFLS NNSFVGEIPT NLTYCSNLKL LFLSGNHLIG KIPTEIGSLK
KLQAMTVAHN NLTGGIPSFI GNLSCLTRLS AALNNFEGDI PQEICCRKHL TFLALGENNF
SGKIPSCLYN ISSLISLAVE QNNFLGSFPP NIFHTLPNLK IFDFAGNQFS GPIPFSIANA
SALQILDLSE NMNLVGQVPS LGNLQDLSIL NLEENNLGDN STMDLEFLKY LTNCSKLHKF
SISYNNFGGH LPNSIGNLST ELKQLYMGGN QISGKIPAEL GSVVGLILLT MESNCFEGTI
PTTFGKLKNM QRLHLEENKL SGDIPPFIGN LSQLYDLELD HNMFQGIIPP SLGNCQNLQY
LDLSHNKLRG TIPVEVLNLF SLSILLNLSH NSLSGTLPRE VSMLKNIEEL DVSENHLSGD
IPREIGECIS LEYIHLQRNS FNGTIPSSLA SLKGLRYLDL SRNQLSGSIP DGMQNISFLE
YLNVSFNMLE GEVPTNGVFG NATQIEVIGN KKLCGGISHL HLPPCPIKGR KHAKQHKFRL
IAVIVSVVSF ILILSFIITI YMMRKRNQKR SFDSPTIDQL AKVSYQELHV GTDGFSDRNM
IGSGSFGSVY RGNIVSEDNV VAVKVLNLHK KGAHKSFVVE CNALKNIRHR NLVKVLTCCS
STNYKGQEFK ALVFEYMKNG SLEQWLHPET LNANPPTTLN LGHRLNIIID VASALHYLHR
ECEQLILHCD LKPSNVLLDD DMVAHVSDFG IARLVSTISG TSNKNTSTIG IKGTVGYAPS
EYGMGSEVST YGDMYSFGIL MLEMLTGRRP TDELFKDGQN LHNFVTISFP CNLIKILDPH
LLPRAEDGAR EDGNHEILLP TVEECLVSLF RIGLFCSLES PKERMNIVDV TRELTTIQKV
FLDGEMN
//
