ID E4UXS6_ARTGP Unreviewed; 703 AA.
AC E4UXS6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=MGYG_04973 {ECO:0000313|EMBL:EFR01971.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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 -!- 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; DS989825; EFR01971.1; -; Genomic_DNA.
DR RefSeq; XP_003172382.1; XM_003172334.1.
DR AlphaFoldDB; E4UXS6; -.
DR GeneID; 10027651; -.
DR VEuPathDB; FungiDB:MGYG_04973; -.
DR eggNOG; ENOG502S5WB; Eukaryota.
DR HOGENOM; CLU_005513_3_0_1; -.
DR InParanoid; E4UXS6; -.
DR OMA; KNEYIDR; -.
DR OrthoDB; 2123140at2759; -.
DR Proteomes; UP000002669; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:EFR01971.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000313|EMBL:EFR01971.1}.
FT DOMAIN 375..703
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 703 AA; 80489 MW; 088BE91DEEFBC765 CRC64;
MLMATRPAAD AEKVYDSDNA ASDSLNLYRG AITKLVSALL ATDAASNLSS QINDQTVDLD
LASLYTQLRK GKGSFNYSPY RALVRLVVQK APWRSTLSSR RGNEQTRKLV EERIFGEIKS
CTHKDVGGFD AKYFRNTSWE EKFIDIYKKI RKQDDTGLSD FPDPPIQDDV LDWWFRLQDT
FLMETRGIYY STEGKKSIKD SDADRQVDVL MRVRTGENAV PTHSWKDIRV VGELKQSNYD
KKGTLLQIER SDSFDICDEP ERFFCAIIGY TLMSDDELGL DTFTTLHNDG TRTVSVEDLD
TGEKEPLRLE SMPLSVQLAV VCRGTCCYRT KKYAASKSQD AVKFSWTSAR RQPEVNLLRL
ARQREVEGVA RVIRYRSITS IAELREGLEY LRNTTKHVVL FPTSATAPAV QIVHEAPGLK
HRQRFIFRLR LLEEEKALYS ICSQISQTFK VEQPSQSLWR RLRKPVFTPH GDGPFENRVL
RCLVISPAGK AIHQFDSLEE LLLALRDAIK AHHSLYIKEK ILHRDISENN IIITDPSITN
GYSGMLIDLD LAKELDSGRT GARHQTGTME FMAIEVLRNI DHTYRHDLES FFYVLIWQCA
RSSWKRLGSL KDMPKESLLR KWYTGSFEDI ANAKAGRMGA KGFEYLLLEF PPELEDVKPL
CRELRQILFR FHQGDILTGT PVRSETLYDP IINAFNEAIQ DLE
//
