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Database: UniProt
Entry: A0A1E4TLE5_9ASCO
LinkDB: A0A1E4TLE5_9ASCO
Original site: A0A1E4TLE5_9ASCO 
ID   A0A1E4TLE5_9ASCO        Unreviewed;       692 AA.
AC   A0A1E4TLE5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CANCADRAFT_30703 {ECO:0000313|EMBL:ODV92581.1};
OS   Tortispora caseinolytica NRRL Y-17796.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trigonopsidaceae; Tortispora.
OX   NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV92581.1, ECO:0000313|Proteomes:UP000095023};
RN   [1] {ECO:0000313|Proteomes:UP000095023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV453841; ODV92581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TLE5; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000095023; 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   CDD; cd11651; YPK1_N_like; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095023};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          102..252
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          286..547
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          548..624
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          156..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   692 AA;  77866 MW;  000F921E05ECDD53 CRC64;
     MTDHSTKYCL TPTLSPQQLC DVSLVSRPQT PIVPSDHQAS GTLYNPHESA HDRLAKLEYS
     SLKTPSSNQK SSLYSQNSSD YRLSNSSNTC LNESTDMGSD LFNTEAQVSL TESVAPPKGR
     LYIRIVEARD LHTSATDAKP YVVCTFESNE AYSGVAALST RESRKPSPDG DSTSSRTVSI
     AIPKSKTSSM QSHQNKSVST SSSWKYEATF DVTNPNSELE IQVYDSNDND RFLGFVRFCP
     DLQDEKSHER WYKLLPRTPE DTVSGEIKVS TTHTPINKRH YSPDDFEILR LVGKGTFGQV
     YQVRKRDTQR IYAMKVLSKK VIVQKKEIAH TIGERNILVR TSSTVSPFIV SLKFSFQTPT
     DLYFVTDYMS GGELFWHLQR EGRFSEERAK FYIAELILAL QHLHSNNIVY RDLKPENILL
     DANGHIALCD FGLSKADLPS NMTTNTFCGT TEYLAPEVLL DDSGYTRMVD FWSLGVLIFE
     MCCGWSPFYA EDTQQMYKNI AFGKVRFPKD ALSSHGRNLV KGLLNRNPNH RLGAVNDAQE
     LREHPFFSDI DWNLLLQKKI PPPFKPHVTS EADTSNFDPE FTGVSTSALN RAYIGSGSTP
     LSPGVQANFQ GFTFVDESAM SYNYRSARGP IDTEMDFIEE DDDSLNDPMP QRQGHASLDY
     DDVDDADGAR RMSGIETMND DDHFIPSEHF II
//
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