ID A0A0D2FRU4_9EURO Unreviewed; 729 AA.
AC A0A0D2FRU4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=Z518_05758 {ECO:0000313|EMBL:KIX04887.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX04887.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX04887.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX04887.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN847478; KIX04887.1; -; Genomic_DNA.
DR RefSeq; XP_013272023.1; XM_013416569.1.
DR AlphaFoldDB; A0A0D2FRU4; -.
DR STRING; 1442369.A0A0D2FRU4; -.
DR GeneID; 25293829; -.
DR VEuPathDB; FungiDB:Z518_05758; -.
DR HOGENOM; CLU_334374_0_0_1; -.
DR OrthoDB; 2123140at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR38248:SF2; FUNK1 11; 1.
DR PANTHER; PTHR38248; FUNK1 6; 1.
DR Pfam; PF17667; Pkinase_fungal; 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 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 312..593
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 249..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 82858 MW; DF6F871456717BC6 CRC64;
MSKNAKFTET QIKRAEEALK TSNEWKKWRS DMISTSSGIT SQNIFFRMLQ KAQEVLQAQS
TAKTRQAHNV FINIGTKVPG SGISNQDYAE GLKLFRPDLA SIATNVDKEN VRFCDMKTTW
ELKKSADQTF AQSEIQLSLL GCNQVFRDDP FRHFIYSIYV AGTTLRLYQL NRGQVLCYES
GLNIEQNTLS FLRFVNWLML ASDDAQGLAE EPSVIGRRAI SFTLAECKIP SPLVRVGVDM
VTTRGTTVWP VKMQKPKPKK KKSRKSQAKK DTENPEGGGL AALKMAWIHE ARTGEADILS
ELSDIEELPK LFEWKDGPLT TEFDVLPEAK HSRQYLKIGP KYRYMKVTHT KSSATANQTQ
KKEAEKGLLV PEVNETAIEP VDEPSYTRRQ RWYLEEYCGV SVDTTPYGLS QHQYPNPRDV
TELERMKALR SAVRAIRKMF CRDRPIIHRD ISPANIMVTS PDILNEERAP PPGRLIDLDM
ACIYGDPYSG APWRTGTYLY MAINILMAKH PRHNPWHDIE SVFWVLLFGE LNRTPEGAEE
LEDIASAGAS RPTEAKKGVG LASRKNLIVS VTWNTWMSDE RLRLFEKTSF PVIRLMHRLR
VELFGFDEQK EPDRLATSED VAAVASKRII TSTEYDAPRF AVPNEKIWEK AEKEVEEVER
GIEGLSLEEK ADKTNQGKSN DSADKGGVEM SEKDLAIERL KQAVTKVTER IDGWFAECIE
DLENVEQQE
//
