ID A0A396IB06_MEDTR Unreviewed; 772 AA. AC A0A396IB06; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 14-DEC-2022, entry version 20. 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; 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: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, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00001433, CC 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|ARBA:ARBA00000775, CC ECO:0000256|PIRNR:PIRNR000641}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A396IB06; -. DR Proteomes; UP000265566; Chromosome 4. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. 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; PK_Tyr_Ser-Thr; 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; alpha-D-mannose-specific plant lectins; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR000641}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641}; KW Tyrosine-protein kinase {ECO:0000313|EMBL:RHN61971.1}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..772 FT /note="Receptor-like serine/threonine-protein kinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5017478094" FT DOMAIN 24..144 FT /note="Bulb-type lectin" FT /evidence="ECO:0000259|PROSITE:PS50927" FT DOMAIN 282..318 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 337..417 FT /note="Apple" FT /evidence="ECO:0000259|PROSITE:PS50948" FT DOMAIN 454..730 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 733..772 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 744..772 FT /note="Polar residues" FT /evidence="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 //