ID A0A1Q8RQ84_9PEZI Unreviewed; 306 AA.
AC A0A1Q8RQ84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CCHL11_08441 {ECO:0000313|EMBL:OLN86489.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN86489.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN86489.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN86489.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) 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}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000256|ARBA:ARBA00010630}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLN86489.1}.
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DR EMBL; MPGH01000127; OLN86489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RQ84; -.
DR STRING; 708187.A0A1Q8RQ84; -.
DR OrthoDB; 121617at2759; -.
DR Proteomes; UP000186583; 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; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR12209:SF0; EKC_KEOPS COMPLEX SUBUNIT TP53RK; 1.
DR PANTHER; PTHR12209; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF01636; APH; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186583};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 19..306
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 33669 MW; CF1D54382CBBDBA3 CRC64;
MSQPEGPFPL PPLLTHPSST GPVLITQGAE ARLYKTTFLS SRLPAALKHR PKKPYRHPTL
DARLTRARIL AEARVLAKCR REGCPVPALY ALDEVAGWIM LEWIPGAPVR VRINEYLDSR
FPTRTPLRDI PETTSTSSAA QEDTPMKDQT DPDAQTKPPR ASASTTASPS STTDHPDLKD
LMRRVGAAIG KMHSTGIVHG DLTTSNMMLR PPPESPGTTE AAAATSPLQG DIYIIDFGLA
SQSTSEEDRA VDLYVLERAF GSTHPRAEAF FQDVLDAYRD SYRQAVVTLK KLEDVRMRGR
KRSMIG
//