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Database: UniProt
Entry: N1Q6C5_PSEFD
LinkDB: N1Q6C5_PSEFD
Original site: N1Q6C5_PSEFD 
ID   N1Q6C5_PSEFD            Unreviewed;       251 AA.
AC   N1Q6C5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=EKC/KEOPS complex subunit BUD32 {ECO:0000256|ARBA:ARBA00019973};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Atypical Serine/threonine protein kinase BUD32 {ECO:0000256|ARBA:ARBA00030980, ECO:0000256|ARBA:ARBA00033194};
DE   AltName: Full=EKC/KEOPS complex subunit bud32 {ECO:0000256|ARBA:ARBA00013948};
GN   ORFNames=MYCFIDRAFT_26109 {ECO:0000313|EMBL:EME87834.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME87834.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME87834.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME87834.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase
CC       activity in the context of the EKC/KEOPS complex and likely plays a
CC       supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex
CC       also promotes both telomere uncapping and telomere elongation. The
CC       complex is required for efficient recruitment of transcriptional
CC       coactivators. {ECO:0000256|ARBA:ARBA00003747}.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC       CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC       {ECO:0000256|ARBA:ARBA00011534}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC       {ECO:0000256|ARBA:ARBA00010630}.
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DR   EMBL; KB446555; EME87834.1; -; Genomic_DNA.
DR   RefSeq; XP_007919732.1; XM_007921541.1.
DR   AlphaFoldDB; N1Q6C5; -.
DR   STRING; 383855.N1Q6C5; -.
DR   GeneID; 19338470; -.
DR   KEGG; pfj:MYCFIDRAFT_26109; -.
DR   eggNOG; KOG3087; Eukaryota.
DR   HOGENOM; CLU_063953_0_0_1; -.
DR   OrthoDB; 121617at2759; -.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR022495; Bud32.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; TIGR03724; arch_bud32; 1.
DR   PANTHER; PTHR12209:SF0; EKC/KEOPS COMPLEX SUBUNIT TP53RK; 1.
DR   PANTHER; PTHR12209; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF06293; Kdo; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          26..251
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  28132 MW;  98672F9D9CC0941D CRC64;
     MTTDTNTDLA SHPPRSLPPP FNNSPLSAFQ LIAQGAEALL YKTQFLTPTQ SAALKVRPKK
     PWRHPTLDRR LTRQRILAEA RVLVKCLREG VKVPQIYALD WEQGWMVSEW IEGPGTVKAV
     IRGWEAGEDE LRSLLRRIGA AVGKLHDIGV VHGDLTTSNM MLRATSDDGP DETEEVVLID
     FGLAVQNATM EEDRAVDLYV LERAFGSTHP KEERLFDEVL NGYEGSFKGA KKTLKKLEDV
     RMRGRKKSMI G
//
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