ID   Y4407_SELML             Reviewed;         567 AA.
AC   P0DH62; D8S6A6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Inactive protein kinase SELMODRAFT_444075;
GN   ORFNames=SELMODRAFT_444075;
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-286 AND 348-567.
RA   Richardson P., Lucas S., Rokhsar D., Wang M., Lindquist E.A.;
RT   "DOE Joint Genome Institute Selaginella moellendorffii EST project.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFJ20033.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes.; Evidence={ECO:0000305};
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DR   EMBL; GL377604; EFJ20033.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; FE450848; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FE450849; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_002979076.1; XM_002979030.1.
DR   AlphaFoldDB; P0DH62; -.
DR   SMR; P0DH62; -.
DR   PRIDE; P0DH62; -.
DR   KEGG; smo:SELMODRAFT_444075; -.
DR   InParanoid; P0DH62; -.
DR   OrthoDB; 684563at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..567
FT                   /note="Inactive protein kinase SELMODRAFT_444075"
FT                   /id="PRO_0000412059"
FT   DOMAIN          255..487
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          148..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         261..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   567 AA;  63194 MW;  DED72F5376FB69D8 CRC64;
     MVMEKLRKIH DLKKVHTTLE ILQFARRGVI PSEAKRFRAT WVVLDRNLKS EGKLCLQELN
     SNIVVVHRSN PKILRLNLKR RDLPYDEEES IDSSSVLLNG LSLSVMPKGF DQLYWESSTS
     SSEASSPDSR LVTAPKFELS VLEELLKNET RRKGPSPSEV LNSTTSSPAS HKPQVLNDFL
     RMKESREYTE ETDTQRNVSR PVDRVSSVRK QIHLRKQSSP QPPPLCSICQ HKTPVFGKPP
     RKFTFAELQL ATGGFSDVNF LAEGGYGSVY RGRLPDGQAV AVKQHKLAST QGDKEFCAEV
     EVLSCAQQRN LVMLIGYCAE DKKRLLVYEF VCNGSLDSHL YGRRSKTVGD FGLARWQPNG
     ELGVETRVIG AFGYLAPEYT QTGQITEKAD VYSFGIVLLE LVSGRKAVDL SRNKGEMCLS
     EWARPFLREQ KYEKLIDQRL RGRFCVNEVE NMLLAATLCI DPDPLIRPRM SQVLRLLEGD
     SLSDTSLSSS SSGLLNGSPV SILLIGDLSQ DSSSSRSSSA SSVLKSFSRT QHSSRSSSNA
     GSPLNPAATQ ALAFKKYNKN TTRHTQD