ID A0A087GS31_ARAAL Unreviewed; 975 AA.
AC A0A087GS31;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=AALP_Aa6g275300 {ECO:0000313|EMBL:KFK32683.1};
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:KFK32683.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM002874; KFK32683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GS31; -.
DR EnsemblPlants; KFK32683; KFK32683; AALP_AA6G275300.
DR Gramene; KFK32683; KFK32683; AALP_AA6G275300.
DR eggNOG; ENOG502QPTD; Eukaryota.
DR OMA; IPLKNEC; -.
DR OrthoDB; 1210969at2759; -.
DR Proteomes; UP000029120; Chromosome 6.
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 CDD; cd14066; STKc_IRAK; 1.
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; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF281; OS06G0186100 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 10.
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; 9.
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}; 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:UP000029120};
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 589..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 656..955
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 975 AA; 107959 MW; E4BA9BBFBA3410B0 CRC64;
MTVLASKEKD HEFIKNDQIS LLSFKSSIVS DPHNSLSTWI PSSSFVDVCN WFGVKCNNES
TRVTELDISG IDLRGEISPS IANLTALTVL DLSRNFFSGQ IPPEIGLLYK TLKQLSLSEN
LLQGNIPQEL GLLNHLVYLD LGTNRFTGQI PVQLFCNGSS LSLQYIDLSN NSLTGEIPLK
NHCHLKELRF LLLWSNKLDG NVPSSLSNST NLKWIDLESN LLTGELPSQV ISKMPQLQFL
YLSYNHFVSH NNNTNLEPFF ASLANSSDLQ ELELAGNNLG GEIPSSVRHL SVNLVQIHLD
QNRIHGSIPP EISNLSNLTL LNLSSNLLTG PIPRELCKLS KLERVYLSNN RLSGEIPVEL
GDIPHLGLLD LSRNKLSGSI PDSFANLSQL RRLLLYGNHL SGTVPQSLGK CINLEILDLS
HNNLTGKIPV EVVSNLRNLK IYLNLSSNHL SGAIPLELSK MDMVLSIDLS SNEFSGKIPP
LLGSCIALEH LNLSRNGFFG PLPASVGQLP YLKELDVSLN SLTGDIPSSF QQSSTLKHLN
FSFNLFSGNV SDKGSFSKLT IESFLGDSLL CGSIKGMRVC KKRRKYPAVL LPVLLSLIAT
PFLCFFGYPL VLKARFGKNL TVYDQEEIED EEKQNRKDPN YPRISYQQLI EATGGFSDSN
LVGSGRFGHV YKGVLRNNTK IAVKVLDPKT ALEFSGSFKR ECEILKRTRH RNLIRIITTC
SKPGFKALVL PLMPNGSLEK HLYPEEYSSR DLDLIQLVSI CSDVAEGIAY LHHYSPVKVV
HCDLKPSNIL LDDEMTALVT DFGISRLVQG VEETVSTDDS VSFGSTDGLL CGSVGYIAPE
YGMGKRASIH GDVFSFGVLL LEIVSGRRPT DVLVNEGSSL HEFIKSHYPN SLEGIVEHAL
IRWKPQGKPE KCEKLWREVI LEMIELGLIC TQYTPLTRPN MLDVAHEMGR LKEYLFACPS
LVHSQTQETQ GEASS
//
