ID G8BUD8_TETPH Unreviewed; 798 AA.
AC G8BUD8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN Name=TPHA0F02430 {ECO:0000313|EMBL:CCE63724.1};
GN OrderedLocusNames=TPHA_0F02430 {ECO:0000313|EMBL:CCE63724.1};
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:CCE63724.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63724.1, 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).
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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR EMBL; HE612861; CCE63724.1; -; Genomic_DNA.
DR RefSeq; XP_003686158.1; XM_003686110.1.
DR AlphaFoldDB; G8BUD8; -.
DR STRING; 1071381.G8BUD8; -.
DR GeneID; 11535617; -.
DR KEGG; tpf:TPHA_0F02430; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_000288_46_2_1; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000005666; Chromosome 6.
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; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 93..348
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 680..773
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 798 AA; 92695 MW; 633A8D5280BB7490 CRC64;
MVLAPLQVVT DNQKVNRIEN FKKSNNNNYI NEDYINIKNT SKISYNENDV VQVINKKDNL
IKQNNEKLNR KKEKTNLLCK TPPSVIKDNS KKYFRRECLG EGGFARCFHI KDDVGISFAC
KIVSKKSIKT ERTKFKLLSE IQIHQNLRYS HIVKFMDCFE DELNVYILLE LCPNGSLMDL
LKKRKILTEA EVKFMTTQVC GAINYMHSNN IIHRDLKLGN VFFDKNFNIK IGDFGLAATL
SNVSEKKYTM CGTPNYIAPE VILSKQIGHS FEADIWSLGI MIYAMVLGKP PFQAKDVTTI
YEKIKLCQYE FPPDKYITND VKVLIQDLLV LDPSQRPRIM DILKYNWFKH SFPPKLPSTI
FTEVPLYFIE LSTLNSLKHF KNCLISCQLI VDLSKNNKTP FHNVFLNERQ NIKNNPINTN
LTNNNDVLQF CDTSFNSNNN NQVRKSEKIR KMNELNDDIR TNVLNPIGTT NLIKSRNAIK
ILNKACLDTL TTLLKIEQYN YNIKLDEIEQ DEWATQKMPI IITKWVDLTT SSIKSSIFHN
PKATENCFIY QLSTEDIGVL KSNGTTILKL FDVPEYWLIE TDFKVGWIAK HKQYNDNSKK
NTNYNTTVST SMTTSNSLNS NKDNLNDQNR MEARTEEINT KKNMVFVEKY EEYMNKNLTR
VSTFVKQKYH KDDIFLRRFT RCKEFVMFEL SDCGFQFNFK DHFKIVLSDN GHIISIITPK
QDSFVLSTKH FLSVAKYLNA NPKSTNLETV YLNTISYGSC SQQEVKNKLK KLKFNQLKIL
EKIEMIKNIL NQKSHGTI
//
