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Database: UniProt
Entry: D8T084_SELML
LinkDB: D8T084_SELML
Original site: D8T084_SELML 
ID   D8T084_SELML            Unreviewed;       959 AA.
AC   D8T084;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=SELMODRAFT_129007 {ECO:0000313|EMBL:EFJ10037.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ10037.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; GL377657; EFJ10037.1; -; Genomic_DNA.
DR   RefSeq; XP_002989008.1; XM_002988962.1.
DR   AlphaFoldDB; D8T084; -.
DR   EnsemblPlants; EFJ10037; EFJ10037; SELMODRAFT_129007.
DR   Gramene; EFJ10037; EFJ10037; SELMODRAFT_129007.
DR   KEGG; smo:SELMODRAFT_129007; -.
DR   eggNOG; ENOG502QPQ4; Eukaryota.
DR   HOGENOM; CLU_000288_114_6_1; -.
DR   InParanoid; D8T084; -.
DR   OMA; SAIEYLW; -.
DR   OrthoDB; 1210136at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
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; 2.
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; PTHR47986:SF13; OS04G0685900 PROTEIN; 1.
DR   PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
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:UP000001514};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..959
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003123202"
FT   TRANSMEM        507..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          611..891
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          468..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   959 AA;  101655 MW;  6C51D3585F0A68FF CRC64;
     MKLKKKHPAA LLLLLVASIL AMALAQTDSA ELQVLQNFLK GVKNPALLDS WTGSDPCGSN
     WKHIKCQGSS ISALQVAGLA LGGTVAPDLN KLKNLENLQL QGNGFTGSLP SLSGLSQLQT
     ALLSGNSFDT IPGDFFTGLS ALTEIYLDDN PLNKSSGGWM LPAEIQNSSL LSTLSITNTS
     LGGSIPDFLG QMESLKVLNV AYNRISGGIP SSFGSSNLAE FRANNQQNPV LSGPITVVGT
     MQSLRVLWLH VNRFSGSIPE GLGEALSLQE LKLNDNQLTG TIPPSLANLP ALKNFTVKNN
     LLVGEIPVFK DTVGFEYARN NFCKSSPGEA CARDVTALLH FLAGVGYPDS LTSSWIGNDP
     CGTSGSNGSS GSAWLGISCG STPGTTSNVT VINLASSQLN GTLSAALGNL TTLTTLRLSD
     NKLEGLIPES LAKLPSLQSV DLSNNLFSAP VPAFPSSVKL NIAGNPLTPA ASPGTSPPGG
     TSGGPAATPD GQATATTRSK RVNAGPIVGV VVGLVALLLV LFGICLLVYK KKGRKFLRLQ
     GSNTVVVHPR TDNSSDDPEV VKIVVNNNMI TSDNSDTQSR ANSGPSDHVQ VVEAGNLVIS
     IHVLREATKN FSEATILGRG GFGVVYKGVL DDGTAIAVKR MESNCVVSNK GLGEFQAEIA
     VLTKVRHRHL VALLGYCIEG NEKMLVYEFM PQGTLSQHLF EAAKCGYPPL DWKQRLSVAL
     DVARGMEYLH GLAHRSFIHR DLKPSNILLG DDLRAKVSDF GLVKLAPEGK YSVETRLAGT
     FGYLAPEYAV TGRVTTKADV FSFGVVLMEL ITGRRALDET QAEENMHLVT WFRRSTANKE
     GVRKLIDPAI ESDDNFASIS VVAELAGHCT AREPYQRPDM GHAVNVLSPL VEHWKPVDYE
     DESGGIDLDV PLPQAVKRWQ ELDSGGGGGG AAAVWSDTQS SLPPRPSGFA ETFTSEDAR
//
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