ID I2H5P5_TETBL Unreviewed; 510 AA.
AC I2H5P5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Meiosis-specific serine/threonine-protein kinase MEK1 {ECO:0008006|Google:ProtNLM};
GN Name=TBLA0F01550 {ECO:0000313|EMBL:CCH61697.1};
GN ORFNames=TBLA_0F01550 {ECO:0000313|EMBL:CCH61697.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH61697.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH61697.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005575}.
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DR EMBL; HE806321; CCH61697.1; -; Genomic_DNA.
DR RefSeq; XP_004181216.1; XM_004181168.1.
DR AlphaFoldDB; I2H5P5; -.
DR STRING; 1071380.I2H5P5; -.
DR GeneID; 14496806; -.
DR KEGG; tbl:TBLA_0F01550; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; I2H5P5; -.
DR OMA; FIQYKGG; -.
DR OrthoDB; 1451820at2759; -.
DR Proteomes; UP000002866; Chromosome 6.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd22670; FHA_MEK1-like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 74..129
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 179..490
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 510 AA; 58507 MW; 2B5689AC53B7CEFB CRC64;
MLKKETSILN IFFKKQMCTN SMRTQLGYLN VSSVEVLREV NFSQSQNQYM SSLVEISSKE
HSLVKYEIQR HKILQLGRDG KKCDIVFESS AVSSLHCVFW GILFDESSIP ICYIKDSSLN
GTFLNGLRLV KDESYVLKDG DIITMKSCDK KLTFNSVQPL PDINVFEALN FQQHVSKWTI
SSNIIGSGTF GHVIVAYKND NEKYHHLENN NKIQINDINE NDEDMCPINY AVKIIKLKPQ
KLDKEAKILF GLNHPNIIKI YYTFCDIRDN LYIFQDLISG GDLFSYLAKG NQLSSLPEPE
SLFIVYQILN ALDYLHGKNI VHRDLKLDNI LLCSPEPYTK IVLADFGIAR NIPDLTENKK
LNKFKETNRM STVVGTPEYC APEVGFKTNR QNYHKFNRAA TLEQKVGYNQ KCDLWSLGVI
THIILSGISP FYGDGSENSI IENTRLGKLN FEVLQWKNVS KNAKDFVSKL LKINVELRLS
AKEGLEHLWI SKHQYVLQKV YDKKKIRGEN
//
