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Database: UniProt
Entry: A0A2V0P853_9CHLO
LinkDB: A0A2V0P853_9CHLO
Original site: A0A2V0P853_9CHLO 
ID   A0A2V0P853_9CHLO        Unreviewed;       781 AA.
AC   A0A2V0P853;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=TKL kinase {ECO:0000313|EMBL:GBF94040.1};
GN   ORFNames=Rsub_07308 {ECO:0000313|EMBL:GBF94040.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF94040.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF94040.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF94040.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBF94040.1}.
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DR   EMBL; BDRX01000047; GBF94040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0P853; -.
DR   STRING; 307507.A0A2V0P853; -.
DR   InParanoid; A0A2V0P853; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GBF94040.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          213..751
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   781 AA;  76725 MW;  DE3336CA157A22B2 CRC64;
     MGAAAASAAP DGPAVATPGA AAAAAAPAAS PKPPARAPNP GLLFEVLQED DDSKRQERLV
     RASIDLAPGA AGRSARASNC SSTSTSAADR RASLASDGGW GGGGGGGGGG APAGTPPRAA
     GGSLEAAFAA AGAAAAAAAA ASPASAPLSP PSPPLLPAAA AAQPDAGGAD AQRGADGAGA
     SPPAGGGGGG GGMTPAEVLQ ELLGPLYVDA STLKMGELLG QGGFAEVRAA ALPDPALPGF
     DEPVAVKALR PDALRSPAEL REFLAEANLL RKMAHPHIVR LRGVGAADLS DLIAMRESMV
     VVQELMAGGD LKGLVSGAMA RPFDPPYTKV DALRWAMQIA EAMQYLHGVC RPMIIHRDLK
     LDNVLLTGGP LHSAAAKLAD FGLHKRVRTI LQSGLALPWA QDVCLQGDAC EKSYYGGGMY
     LAAASGRPGL PPGPTPGLPP APDAPPGLPR VASAGGALGR VCEDGGAVDL GGGGGALAGA
     DLATRVLSST GVGDASRSAS RSRSRGGAAA AAPPVAAAAE EAAAREASVH RRLTAVRALE
     GSVRAGNAFY GGGGADGGGS SSGGGGGGTR QSEIEAWADE EGEAQRPEPA RWSRGGGGGG
     GGGGGGGGGG GGGGGGGASA RGGGGASQRG VLVDATQKVG SLMYMAPEVL RGGGYGEKVD
     VFSYGVMLYE LFSGQLLASR VAMADPQAAA DDGAGGGSGL LAAYAERVAA GHREDLPAYW
     PKALKGLVSD CWAQDPRRRP SFSRVLERLY AMKREGLGEA LDAARPRGNY NPTTDCGCCI
     M
//
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