ID K2RJ72_MACPH Unreviewed; 1326 AA.
AC K2RJ72;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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=MPH_12759 {ECO:0000313|EMBL:EKG10159.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG10159.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG10159.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG10159.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(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}.
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:EKG10159.1}.
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DR EMBL; AHHD01000526; EKG10159.1; -; Genomic_DNA.
DR STRING; 1126212.K2RJ72; -.
DR VEuPathDB; FungiDB:MPH_12759; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_283143_0_0_1; -.
DR InParanoid; K2RJ72; -.
DR OrthoDB; 22648at2759; -.
DR Proteomes; UP000007129; 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 CDD; cd00180; PKc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR11042:SF136; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 1; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 87..371
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 1094..1130
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1177..1209
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1259..1291
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1326 AA; 147588 MW; 522A2B433E75A95B CRC64;
MRPRIYTVLR NIAPERHGDY MDRFADGNYI DFHLPFDNRT LPGFLSNGVM RDNFFNFQHH
VLSPEARSLE IEGGEHQLIA GSADAHFWPL EMLGQGGFGQ VDKVVSRLSC STYARKRIPR
RKDSAVNLRR QNDFVKELEI LKKLSHRHLV TYVGSYTDNH FMAYLMRPVA MWNLLEFLNW
LGDPLNQARR SQVQPYYGCL ASAVGYLHDQ SIRHTDITTR NVLVGEQGKI WLSDFGTATD
FSQSGRSTTN DLIPISIEYS APEVAHRQKR NKASDMWSLG VVFLEITTVL LGNNLGNFGT
FMAKNAKNRD YPQAIWANLP TALDWLARIM SPHVESANEA ITWVRSLLQD DPKNRPTVKN
LMVDIRQTPS FRQFCCLDCW DEFDAGKFEF ETPLNPEGFN ETMKHVTAAE VSARAAALFQ
PQYPPAPIDA DRSKSIEHWI ADSTSATVDT SIIPFPHWVE NRAVDQYQHL GRLSESTDET
ENSLSSTIAT KKKPRYAKEP SRRPMPGAFP EEDVEIGSGF GYVVEDDRTS DGEDPSPKDE
AILAQGFVVE QDSSGSETSD SEVSINLQAC HIVLQRKDEP QPLVQVDSGN QMASHRLGEL
WELMTNDSDQ QGYEKDDYSI GLELGPRNRP DCEALAAESG NSLMLHQSSY DQGRRKPRAI
SERSHDLPET SFSGDFEGFQ QTNDGSKGRQ LYLTWPSQEL ESKVPANQAL PPPPRSIDEP
AHHSPPLPQR GHILQIEYRH EDRSRSLSTA STVSGDVVSE NGSDGSGESD TLLTIPSLEM
QPFGGTTEPP VPKIMQKEDQ SSYTPEENPP VEDFTHEAEP DTLATEIPPK NLQSQQPHRT
REKVHWGQVT IEEIPRDSDD EEEPSAGRNE HRHANKQATV EDAKDASELA PEQNRERQDW
AQTNYASGFG PSDILPMEPL FVEGPTRTAA PAHQSLQSRA HLKALKKDRK RLHQSSKPKD
PSEEAAQQLK RAKRVRKPAP SPTLFMEDAR KAGQHVKSIA TSQMTSRTKQ ALAGCNINRW
VDQTNKLLER YCARGSATAV RTLLAQKCNP GTKAKPRRGP LLKAIQGASA RHSKVVRALL
QYDVDVHVVC PRNYNKTPLH LAIENDDNDG YVNMVHDMVF AGVDPNAKDR NGECALEKIF
KGPESRGLEK YRLDALALLL LSEAKGGTEV NIRVPATRDT PLHLAVRRRS PMAAAMLLHK
GADVNAVNAS GMTPLLSAAL MWRGGSGGTL AQMAPDDEQM LDLLTSQPGI RLNECAGMQR
RTALHHAVVA GVPLAVEILL EKGASLRQRD ADGKTAMGLV ASGRARETSD DKRIRALLSG
ALQLKA
//
