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Database: UniProt
Entry: A0A087HK36_ARAAL
LinkDB: A0A087HK36_ARAAL
Original site: A0A087HK36_ARAAL 
ID   A0A087HK36_ARAAL        Unreviewed;       650 AA.
AC   A0A087HK36;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   OrderedLocusNames=AALP_Aa2g263200 {ECO:0000313|EMBL:KFK42488.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42488.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000327};
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         Evidence={ECO:0000256|ARBA:ARBA00000671};
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DR   EMBL; CM002870; KFK42488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087HK36; -.
DR   EnsemblPlants; KFK42488; KFK42488; AALP_AA2G263200.
DR   Gramene; KFK42488; KFK42488; AALP_AA2G263200.
DR   eggNOG; ENOG502RMXX; Eukaryota.
DR   OMA; RSECICE; -.
DR   OrthoDB; 5479005at2759; -.
DR   Proteomes; UP000029120; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR013695; WAK.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005:SF280; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 10-RELATED; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08488; WAK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..650
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001823413"
FT   TRANSMEM        234..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          307..596
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          628..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  73100 MW;  FDF46A271629F536 CRC64;
     MSSSNNTCSL ILFFFSLLLL LVLDSVALTS LNSCPSKCGD IEIPYPFGIG KDCYLDNGYQ
     IECKNVSRKQ VPFLSISSKE VVNISLPSQF IDGSMSQGSL FIKSPITSSN EQEFGPLFNL
     TGKGNSQWLR AKQYATVEIE WSFRTANLSY ITSLGCIDRS ECICEDRNDS GIIYATCGCK
     HGYRGNPYFL DGCKDIDECH EVDSLDRPLY CYEGSCENLQ GSYGCRYSQL PAPVLSLMIG
     IAMLILIGVG LCLYMCIRRL KRINRKKKLF KRNGGLLLQQ QLTSTQGNVE TTKVFTSKEL
     AKATENFSEK RVLGQGGQGT VYKGMLIDGR IVAVKKSKVV DEDKLEEFIN EVVILSQINH
     RNIVKILGCC LETEVPLLVY EFISNGNLFE HLHDESPDQT MMATTWEMRL RIAIEIAGAL
     SYLHSAASTP IYHRDIKTTN IMLDEKYRAK VSDFGTSRSV TEDHTHLTTL VSGTVGYLDP
     EYFQSSQFTD KSDVYSFGVV LVELITGEKP ISFSRSQENR TLVTYFNLAM KENRVVDIVD
     ARIKDDCKME QVMAVAKVAR RCLNMKRKKR PNMRQVSMEL EMIRSSPEDM QTHEYVSENE
     EEREEEGVEV NIEVDSRNHV AVTSPASQYN VAASSSSWSD VEPLFPSQTH
//
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