ID G8BQ99_TETPH Unreviewed; 685 AA.
AC G8BQ99;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0B00240 {ECO:0000313|EMBL:CCE61696.1};
GN OrderedLocusNames=TPHA_0B00240 {ECO:0000313|EMBL:CCE61696.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61696.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE61696.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612857; CCE61696.1; -; Genomic_DNA.
DR RefSeq; XP_003684130.1; XM_003684082.1.
DR AlphaFoldDB; G8BQ99; -.
DR STRING; 1071381.G8BQ99; -.
DR GeneID; 11534716; -.
DR KEGG; tpf:TPHA_0B00240; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_120_1_1; -.
DR OMA; LMFEMCC; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
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; 1.
DR InterPro; IPR000961; AGC-kinase_C.
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; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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:UP000005666};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 279..538
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 539..614
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 685 AA; 78050 MW; 89948ED8753C1A07 CRC64;
MSEVQIAPEL LSGSSTGNVT PTSGSDSTDR LVTRSGLSRL FNNGNSPNLL NIRYQANEIC
DSEEERDGLP RYDSASYEMS IVDSETDPST TSNINQLSSN ENFTKGILKV NVSGISHYNV
SSHANSLKML ISYDDVSMSS YGRKSSNIEQ AFSSSDTNEN TTSNRFGTWR ENESNNNFNT
NEYLSPIEWS TTIVFDVTND NSNVHISLYN GLQEDRLIGN ASFIPETKYL TTNIIRGWYT
LTGGESSERG DENGEGKYRL YVEYDYQVEH GKKFVPENFE LLKLLGKGTF GRVYQVEKKD
TGKLYAMKVI SKSHIIKKNE IGHTLNERNI LVKNVINSCP FIVNLKYSFQ TNENLYLVTD
FKSGGELFMH LQYCGTFEES RSRFYAAELV LALEYLHDND IIYRDLKPEN VLLDASGNIS
LCDFGLSKLD IKGKTRTFCG TTEYLAPEIL TEKSGYTHMV DFWGLGILMF EMCCGWSPFK
APTIQLVYNN IVFSKIKFPK CNLSQDGRNF IKQLLNRKPD HRLGSNDGAR ELKKHPFFKD
IDWVAMLKKE IEPPFIPILN SDKDTAYFDK EFTKIPKEKL SSHSNYYDNE LSNSMQNCFS
GFTFEEDSIL STNKKQQWIP AAFPEDSDLL MKDVNIETRV SATQEWRTNR LDTTFEPLDL
HDNGNNKYIP LNPSLLRYEG IDSRE
//
