ID A0A498J1S2_MALDO Unreviewed; 1577 AA.
AC A0A498J1S2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DVH24_032026 {ECO:0000313|EMBL:RXH89669.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH89669.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH89669.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH89669.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:RXH89669.1}.
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DR EMBL; RDQH01000335; RXH89669.1; -; Genomic_DNA.
DR EnsemblPlants; mRNA:MD09G0060300; CDS:MD09G0060300.1; MD09G0060300.
DR Gramene; mRNA:MD09G0060300; CDS:MD09G0060300.1; MD09G0060300.
DR Proteomes; UP000290289; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF41; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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}; Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1165..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1227..1508
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 19..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1577 AA; 171139 MW; 7F1C9D586211E6E1 CRC64;
MDDAYRDECG NKHLRVNFES DAVNYRRNSS FPSSSKSSPS SPSSSSSSSP RSSLESFVND
KKDGNNPCVT RTRPDQESQG ALSLPEGYSS PSLPGSMQSG SSAQSSPFQM MGRPAGYDPS
RIPSNIFASK PPAGMDWSVA SNESLFSLHV GNNSFSRDQF ALLNKSGELY KSGELYKSGE
LTRHDEYIYI PTPLPTVTEV ETIEIKIHNV GKEKVENKAP NMEAKIEENE SANVEYKVES
MRENVETESV EETEGPDESA NAKAVKKEKV PLIGEIRNSA ASYQSDGSNN STKSFQFPVL
ENHEVERNIP AEINSGKLQS AHAQQEMHKQ VGTEAQETPL KAATTQTTNF KGKAKDFTPT
AAKMGFSPSS SSVIKGHFFR RPTSPVFVLK LVLLLWVFCS SQNCAVLADT DASVLLELKN
SVLDPSGLLS GWNGRLSSGH CSWTGVFCNS NSRVVSLNLT GNGGETEGRS KTIACSDFSQ
LPLYGFGIRR SCEGSRGRLA GKLPSVIGKL TELRVLSLPF NGFYGEIPSE VLGLENLEVL
DLEGNSVTGS LPFQLNPNLR VLNLGFNMIK GEIPTSWSNY MSLEILSLAG NLVNGTVPGF
IGRLKAVYLS YNSLSGDVPS EIGANCGKLE HLDLSGNFLV HNIPSSLGNC SQLRTLLLYS
NMFEEGIPAE LGRLQALEVL DVSRNTLSSS LPRELGNCSQ LSVLVLSSMF NPLPRGNDTV
VDSLLEQSNA MNDDFNYFQG TMPVEITTLP KLRILWAPRA SIEGTFPSNW GGCEYLEMIN
LAQNFLTGEF TSGLSRCRKL QFLDVSSNRL SGELVQDLHV PCMVMFDISR NMLSGSIPEY
FNRTCASPFG DFSFKSEDPS STYVAFFASK SQVGNPLQMH GEGDSLIVVH NFAHNNFTGA
LQTLPIAPER LGKQTFYAFF AGENKISGEF PGKLFGKCEG LEWLIVNVSH NKLEGQIPAE
VGTMCKSLKG LDASRNQIIG PIPSTIGKLS LVALNLSWNM LRGEIPTSLG QIRNLMYLSL
SGNLLTGVIP SSLGQLTSLE VLELSSNHLT GEIPKDLVNL RNLTVLLLDR NNISGQIPSG
LANVTTLSSF NVSFNNITGS LPANNNLMKC NAAIGNPNLD SCPMFSLAQP ASDSQGRVGD
SQPFAASPVG GPAQKTGNGF NSIEIASITS ASAIVLVLIA LVILFLYTRK WNPKSGTQGS
TRKEVTIFTN IGVPLTFENV VGATGGFNAS NCIGNGGFGA TYKAEISPGI VVAIKRLSVG
RFQGVQQFHA EIKTLGRLRH PNLVTLLGYH ASDTEMFLIY NYLAGGNLEK FIQERSTRAV
DWRVLHKIAL DIARALAYLH DQCVPRVLHR DVKPSNILLD DDFNAYLSDF GLARLLGTSE
THATTGVAGT FGYVAPEYAM TCRVSDKADV YSYGVVLLEL LSDKKALDPS FSSYGNGFNI
VQWSCMLLRQ GRAKEFFTAG LWDAGPHDDL VEVLHLAVVC TVDSLSTRPT MRQVVRRLKQ
LQPPSSLLPA RQTRGSFVRH GGIKTDSTLL LRPEGPKEVR HCCMGSTAGS WHAGPRDAVF
STTCGELSRG VSNFSPR
//
