ID A1D5Z6_NEOFI Unreviewed; 277 AA.
AC A1D5Z6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=NFIA_063010 {ECO:0000313|EMBL:EAW21140.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21140.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 -!- 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; DS027690; EAW21140.1; -; Genomic_DNA.
DR RefSeq; XP_001263037.1; XM_001263036.1.
DR AlphaFoldDB; A1D5Z6; -.
DR STRING; 331117.A1D5Z6; -.
DR EnsemblFungi; EAW21140; EAW21140; NFIA_063010.
DR GeneID; 4589717; -.
DR KEGG; nfi:NFIA_063010; -.
DR VEuPathDB; FungiDB:NFIA_063010; -.
DR eggNOG; KOG3087; Eukaryota.
DR HOGENOM; CLU_063953_1_0_1; -.
DR OMA; HKLYMEY; -.
DR OrthoDB; 121617at2759; -.
DR Proteomes; UP000006702; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAW21140.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 20..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30964 MW; 0EB0E311816947C2 CRC64;
MASADPYTPP PLPSPFTNTT PPPQLLTQGA EAHLYKTVFL SPSTPAALKV RPSKPYRHPI
LDRRLTRQRI LQEARCLVKL VREGVNVPAV LALDWEGQSG EKGFGGAWLM MEWIEGLVVR
VVLERWEKYM KRNQAGQGAE ELKKEEARVR DLMRRIGHAV GALHKAGVIH GDLTTSNLIL
RPPSHAEQQP AADETNPSME GDVVLIDFGL ASQSLQDEDR AVDLYVLERA FGSTHPRTEP
LFEEVLKGYK ESYKGASSAL KRLEEVRMRG RKRSMIG
//
