ID A0A087HRQ1_ARAAL Unreviewed; 2434 AA.
AC A0A087HRQ1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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_Aa1g305000 {ECO:0000313|EMBL:KFK44803.1};
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:KFK44803.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CM002869; KFK44803.1; -; Genomic_DNA.
DR EnsemblPlants; KFK44803; KFK44803; AALP_AA1G305000.
DR Gramene; KFK44803; KFK44803; AALP_AA1G305000.
DR eggNOG; KOG1187; Eukaryota.
DR OrthoDB; 991910at2759; -.
DR Proteomes; UP000029120; Chromosome 1.
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; 2.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 3.
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; IPR021720; Malectin_dom.
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; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF29; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF11721; Malectin; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 3.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 3.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 3.
PE 4: Predicted;
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW 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|SAM:SignalP};
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 SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2434
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001823736"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2081..2103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 683..934
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1240..1524
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2141..2414
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 711
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 2169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2434 AA; 269391 MW; 711F62034E565751 CRC64;
MSSMVFWTFL TFFTIMASFL ATLTTSTSSP TLHPNELNAL KEIATTFGIK RLNLSYVDPC
NSGTLMIIQE VDFVLNPNTN NTILCDCTFN NNTICHITKL FLTTMSLPGK LPPQLVKLRY
LQSIDVYRNY LWGTIPMEWA SMQYLTFISL SSNRLSGKLP IGLQNFKNLK TLWLEANQFS
GQIPDELGNL TNLTVLVLAS NQFTGSLPST LARLVKLKDF RVSDNNFNGT IPGYIGNWTR
LKKLHLYASG LKGPIPDAVA RLENLTELRI SDTTGINSFP NISSQVIKQL ILRNVGLLGS
IPAYIWKMPI LKTLDLSFNN LTGEVQGGQD APRYTYLTGN MLSGNIESGA LLNIKSNIDL
SYNNFSWSPS CQEKSYINKY NSSYLKNNIT GLLPCAGPIN CRKYQRSLHI NCGGDDITIT
RSWGKITYQA DNNQTTAATN QHLANWGISN TGDFNDDATT DDTYFISAAP GDFSDLDKNT
RQSGDSPDLY KTARRSALSL TYYASCLENG LYNVTLHFME IQFSEKELYG HVGRRIFDVY
VQGVLFMKDF NIKEKANGTL TPVVINKAAN VTNHMLEIRL YWAGKGTTVI PIRGNYGPLI
SAISLCHSLE PRCGAEKKKH HTNYPLIFGL TGVLITIILL ALGIYAQKRC RGNKNMRERD
LRAQSLQTVC FSWRQLQAAT NNFDQANKLG EGGFGSVFKG EMSDGTIVAV KQLSSKSCQG
NREFVNEIGM ISGLNHPNLV KLYGCCVEKN QLLLVYEYME NNSLALALYG KSSLKLDWAA
RQKICVGIAR GLEFLHEGSL IRMVHRDIKT SNVLLDADLN AKISDFGLAR LHEEEHTHIS
TKVAGTIGYM APEYALWGHL TEKADVYSFG VVAMEIVSGK SNTNQKGNAD DVSLINWALT
LQQTGDIMEI VDPMLKVNAL KEIATTLGIK RLDLSDGDPC SLGKLKIIPE VDFVPNPNII
NTIVCDCTFN NNTICHITEL YLKTMSLPGK LPPKLVKLRN LQLIDLSTNY LSGTIPMEWA
SMKYLTSISL RGNRLSGTLP IGLQNLKNLT YLGLEANQFS GQIPDEFGNL TNLTGLELAS
NQLTGSLPST LSRLINLETF RICDNNFTGT IPKYIGNWTR LKRLILRNVG LSGPIPSYIW
YMPVLKALDL SFNNLTGDVQ GGQNTPKCTY LTGNMLSGNI ESGALLNSKS NIDLSYNNFS
WSPSCQEKRY KHEILIDLRA QSLQTVCFSW RQLQAATNDF DQANKLGEGG FGSVFKGEMS
DGTIIAVKQL SSKSCQGNRE FVNEIGMISG LNHPNLVKLY GCCVEKDQLL LVYEYMENNS
LALALYDKSS LKLDWAARQK ICVGIARGLE FLHQDSMIRM VHRDIKTSNV LLDADLNAKI
SDFGLARLHG AEHTHISTKV AGTIGYMAPE YALWGHLTEK ADVYSFGVVA MEIVSGSNIT
KHKGNADHAS LINWALALQQ KGDILEIVDP MLEGEFNSNE STRMIKVALV CTNSSPTLRP
TMSEAVQMLE GEMEIPQVIS DPALHPDELK ALEKIGTTLG IKGLNLSYED PCKSGTLKMI
VPNQDFRNNT IRCNCRFDNN TICHITSIDL KSLSLPGTLP PEFADLPYLQ SINLLSGTIP
LEWASLPYLT YISVCANNLS GTLPIGLQNF KNLTFLGLEA NQFSGQIPDE LGNLTNLGSL
HLTSNQFTGS LPTTLARLVN LTDFRVSDNN FNGTIPGYIG NWSGLRRLHL YASGLKGPIP
DAIGSLENLV DLRISDTTGI NSFPNISSKA IKTLTLRNVS LSGLIPSYIW DIEELIVLDL
SFNKLTGEVS GVQRAPKYTY LTGNKLSGDP GSGVFLNSQS NIDVSYNNFS WSSSCQENSN
INTYRSSYIK NNLTGLLPCE SPITCTSYQR TLHINCGGEN IVVTNSSHKI TYQADNSQTN
AASNQHFENW GISNTGVFFT NAPDLYDEDD TYIISPRLTL AGDIPDLYKT ARRSPISLVY
YAFCLENGDY DVKLHFMEIQ FSDKEPYSSL GRRIFHVYVQ GELFLKDFNI KEEANGTLTP
VVKVKKTVNV TDHTLEIRLY WAGKGLEPRC GAEKTKDPSN YALIFGVTGA LVTVTVLALG
LYVQRRCRGD KNTRERVDLR AHSLQTVCFT WRQLQAATNN FDQSNKLGEG GFGSVFKGEM
SDGTIIAVKQ LSSKSCQGNR EFVNEIGMIS GLNHPNLVKL YGCCVENNQL LLVYEYMENN
SLALALYGKS TPKLDWAARQ KICVGIARGL EFLHEGSMIR MIHRDIKTTN VLLDADLNAK
ISDFGLARLH GGEHTHISTR IAGTIGYMAP EYALWGHLTE KADVYSFGVV AMEIVTGKSN
GTMKGGNDSL SLINWAFTLQ QKEDIAEIVD PMLKGDFNSK EAMRMINVAL VCTNSSPSLR
PTMSEAVQML EGEIEITQVM SDPSMNDDND ILSV
//