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Database: UniProt
Entry: D8TBB6_SELML
LinkDB: D8TBB6_SELML
Original site: D8TBB6_SELML 
ID   D8TBB6_SELML            Unreviewed;      1095 AA.
AC   D8TBB6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=SELMODRAFT_136102 {ECO:0000313|EMBL:EFJ06059.1};
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:EFJ06059.1, 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; GL377708; EFJ06059.1; -; Genomic_DNA.
DR   RefSeq; XP_002992868.1; XM_002992822.1.
DR   AlphaFoldDB; D8TBB6; -.
DR   EnsemblPlants; EFJ06059; EFJ06059; SELMODRAFT_136102.
DR   GeneID; 9646120; -.
DR   Gramene; EFJ06059; EFJ06059; SELMODRAFT_136102.
DR   KEGG; smo:SELMODRAFT_136102; -.
DR   eggNOG; ENOG502QUMP; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; D8TBB6; -.
DR   OMA; ITVVATW; -.
DR   OrthoDB; 457890at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48052:SF59; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48052; UNNAMED PRODUCT; 1.
DR   Pfam; PF00560; LRR_1; 14.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-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}; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1095
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003123451"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          766..1036
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         795
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1095 AA;  119296 MW;  99EA82DD6B1B1744 CRC64;
     MLVRKLCFIV VTVAALIRCC AADPPEQEAL REFLLAAKGS ELLKSWSTSS SSPCSWLGVS
     CSSNGHVVEL SLGGLPLYGR IPTVFGFLSE LKVLNLSSTN LTGSIPEELG SCSKLQLLDL
     SVNSLTGRVP SSIGRLKELR SLNLQDNQLQ GSIPKEIGNC TSLEELQLFD NQLNGSIPPE
     IGQLGKLQAF RAGGNMALSG PLPPELSNCR NLTVLGLAVT ALSGSIPGSY GELKNLESLI
     LYGAGISGRI PPELGGCTKL QSIYLYENRL TGPIPPELGR LKQLRSLLVW QNAITGSVPR
     ELSQCPLLEV IDFSSNDLSG DIPPEIGMLR NLQQFYLSQN NITGIIPPEL GNCSSLTFLE
     LDTNMLTGPI PPELGQLSNL KLLHLWQNKL TGNIPASLGR CSLLEMLDLS MNQLTGTIPA
     EIFNLSKLQR MLLLFNNLSG TLPNNAGNCI SLLRLRLNNN MLSGSLPISL GQLRNLNFLD
     LHDNMFSGPL PTGISNLSSL QMLDVHDNQL SGPFPAEFGS LSNLEILDAS FNNLSGPIPA
     EIGKMNLLSQ LNLSMNQLSG NIPPEMGRCK ELLLLDLSSN QLSGNLPPDL GMITSLTITL
     DLHKNRFIGL IPSAFARLSQ LERLDISSNE LTGNLDVLGK LNSLNFVNVS FNHFSGSLPS
     TQVFQTMGLN SYMGNPGLCS FSSSGNSCTL TYAMGSSKKS SIKPIIGLLF GGAAFILFMG
     LILLYKKCHP YDDQNFRDHQ HDIPWPWKIT FFQRLNFTMD DVLKNLVDTN IIGQGRSGVV
     YKAAMPSGEV VAVKKLRRYD RSEHNQSEFT AEINTLGKIR HRNIVRLLGY CTNKTIELLM
     YDYMPNGSLA DFLQEKKTAN NWEIRYKIAL GAAQGLSYLH HDCVPAILHR DIKPNNILLD
     SRYEPYVADF GLAKLIGSST SAADPMSKVA GSYGYIAPEY SYTLKISEKS DVYSYGVVLL
     ELLTGREAVV QDIHIVKWVQ GALRGSNPSV EVLDPRLRGM PDLFIDEMLQ ILGVALMCVS
     QLPADRPSMK DVVAFLQEVK HIPEEASSIK VPAAAPAAAA GDQLSDQMPL FCKNHTASTY
     EFVFDDNSSS QSGGC
//
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