ID A0A396IB06_MEDTR Unreviewed; 772 AA. AC A0A396IB06; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-NOV-2019, entry version 9. DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641}; GN ORFNames=MtrunA17_Chr4g0042381 {ECO:0000313|EMBL:RHN61971.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; OC Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:RHN61971.1, ECO:0000313|Proteomes:UP000265566}; RN [1] {ECO:0000313|Proteomes:UP000265566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566}; RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7; RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S., RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M., RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W., RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F., RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F., RA Benhamed M., Crespi M., Gouzy J., Gamas P.; RT "Whole-genome landscape of Medicago truncatula symbiotic genes."; RL Nat. Plants 4:1017-1025(2018). 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000641}; 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|PIRNR:PIRNR000641}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. {ECO:0000256|PIRNR:PIRNR000641}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RHN61971.1}. 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; PSQE01000004; RHN61971.1; -; Genomic_DNA. DR Proteomes; UP000265566; Chromosome 4. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro. DR CDD; cd00028; B_lectin; 1. DR Gene3D; 2.90.10.10; -; 1. DR InterPro; IPR001480; Bulb-type_lectin_dom. DR InterPro; IPR036426; Bulb-type_lectin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003609; Pan_app. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR021820; S-locus_recpt_kinase_C. 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 Pfam; PF01453; B_lectin; 1. DR Pfam; PF11883; DUF3403; 1. DR Pfam; PF08276; PAN_2; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF00954; S_locus_glycop; 1. DR PIRSF; PIRSF000641; SRK; 2. DR SMART; SM00108; B_lectin; 1. DR SMART; SM00473; PAN_AP; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF51110; SSF51110; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50927; BULB_LECTIN; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50948; PAN; 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|PIRNR:PIRNR000641, KW ECO:0000256|SAAS:SAAS01216376}; KW Complete proteome {ECO:0000313|Proteomes:UP000265566}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Kinase {ECO:0000256|PIRNR:PIRNR000641, ECO:0000256|SAAS:SAAS01216370, KW ECO:0000313|EMBL:RHN61971.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641, KW ECO:0000256|SAAS:SAAS01216382}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641, KW ECO:0000256|SAAS:SAAS01216375}; Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|PIRNR:PIRNR000641, KW ECO:0000256|SAAS:SAAS01216377, ECO:0000313|EMBL:RHN61971.1}; KW Tyrosine-protein kinase {ECO:0000313|EMBL:RHN61971.1}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 772 Receptor-like serine/threonine-protein FT kinase. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5017478094. FT DOMAIN 24 144 Bulb-type lectin. {ECO:0000259|PROSITE: FT PS50927}. FT DOMAIN 282 318 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DOMAIN 337 417 Apple. {ECO:0000259|PROSITE:PS50948}. FT DOMAIN 454 730 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT REGION 733 772 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 744 772 Polar. {ECO:0000256|SAM:MobiDB-lite}. SQ SEQUENCE 772 AA; 86839 MW; E01A7BA64B553380 CRC64; MSFITYILFV LSLIASYSIA SNDTSSITQS QSISDGETIV SPKGLFELGF FSITNPNKRY LGIRFKNIST QNVVWVANGG KPINDSSAIL KLNSSGSLVL THNNNIVWFT NSSTKAQKPV AQLLDTGNLV IKEDSVSETY LWQSFDYPSN TLLSGMKLGW DHKRNLNRRL IAWKSDDDPT PGDFSWGVVL NPYPDIYMMK GEKKYYRLGP WNGLRFSGRP DLKPNDIFSY NFVWNKEEVY YTWNIKDSSQ VSKMVLNQTS KDRPRYVWSK DVESWRVYSR IPGDICDHYG QCGVNGYCSS TNSPICGCLQ GFKPKFPEKW NSIDWSQGCL RNHTLNCTND GFVSVANLKV PDTTYTLVDE SIGLEQCRGK CLNNCSCMAY TNTNISGAGS GCVMWFGDLI DIKLIPGGGQ FLYIRMPASE LGKSKTEGNY ERHIDDLDLP LLDLSTIITA TDNFSEKNKI GEGGFGPVYL GKFESGLEIA VKRLSQSSAQ GMREFINEVK LIANVQHRNL VTLIGCCIQR EEKMLVYEYM ANGSLDYFIF DRTKSKLLDW PKRFHIICGI ARGLMYLHQD SRLRIVHRDL KSSNVLLDDT LNPKISDFGL ARTFGGNQIE GNTNRIVGTY GYMAPEYAID GQFSVKSDVF SFGILLLEII CGKKNRVCHR TKQTLNLVAY AWTFWKHGRP LQIIDSNIVD SCIVSEVSRC IHVGLLCVQQ YPEDRPTMAD VILMLGSEMM TLDEPKEPGF TTRKESAEAN SSSSGKDTSS NYEMTMSSFS AR //