ID   PTK2_CANGA              Reviewed;         777 AA.
AC   Q6FRE7;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine/threonine-protein kinase PTK2;
DE            EC=2.7.11.1;
GN   Name=PTK2; OrderedLocusNames=CAGL0H09152g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CR380954; CAG60130.1; -; Genomic_DNA.
DR   RefSeq; XP_447197.1; XM_447197.1.
DR   AlphaFoldDB; Q6FRE7; -.
DR   SMR; Q6FRE7; -.
DR   STRING; 5478.XP_447197.1; -.
DR   EnsemblFungi; CAG60130; CAG60130; CAGL0H09152g.
DR   GeneID; 2888743; -.
DR   KEGG; cgr:CAGL0H09152g; -.
DR   CGD; CAL0130128; CAGL0H09152g.
DR   VEuPathDB; FungiDB:CAGL0H09152g; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_009275_1_1_1; -.
DR   InParanoid; Q6FRE7; -.
DR   OMA; IPRQSKR; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0000296; P:spermine transport; IEA:EnsemblFungi.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..777
FT                   /note="Serine/threonine-protein kinase PTK2"
FT                   /id="PRO_0000086590"
FT   DOMAIN          222..529
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          21..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         228..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   777 AA;  85717 MW;  56FF1235DE62F7D6 CRC64;
     MTVATEKTPH KSSSMFKLFS NKLRGNNDST PAAAPAPVPT KKLTKAHTSA HISRSASTNT
     PHPLRNGVTG IPSASPAPRQ MTRRSTGVTP TMVKSSKQLS TLTAHNSNPF RNKNGTISSA
     SHTHNGPTNS QHMVYNPYGI NNRPTETQSS VRGSSYSRHG SGSHISSGSA SSTNNNTDLS
     FYMHDGDNKI RMLPLPIADP NEFLPDDIKQ VSIHLSDNFS FDKDNKTIGS GGSSEVRIVR
     SNYRSKDVYA LKKLNMIYDE TPEKFYKRCS KEFIIAKQLS NNIHITSTFY LVKVPTTIYT
     TRGWGFIMEL GSKDLFQLME KSGWKNVPLH EKFCLFKQVA QGVKFCHDNG IAHRDLKPEN
     VLLSKDGVCK LTDFGISDWY HKENEDGTIE VKQNAGMIGS PPYAPPEVMY WDAKKKYPTS
     MQKPYDPLKL DCYSLGIIFI TLINNIIPFF ESCNMDPKFR EYENSYNNFI RYQNKNFRQK
     GTYKPGPGSE YMLARRFKNA DASRVAWRLA DPDPETRYTM EDLFNDPWFQ SVETCVDVND
     VNLVRHPQIK KTSSEGINLV NAADAHPIPS PMVGTDTNGG LHSDSENPAG THTTEESVET
     PKPASIRELH KPRSMVDIAE SPMKKAATTP LFTLDEEAKE ERDHEQETNT TAEADNEKAQ
     TVPTSAVDTN EFASKENATT TDNDNVNTKA TTADPTTQQG AEITETGSIA GSISASISAS
     ITASMSGSVS GAATAPIPRR DPSNRSIHSN ATSTGTAGRK KKVVHHHMEV PGSAFQI