ID V5ELC2_KALBG Unreviewed; 1649 AA.
AC V5ELC2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=N(6)-L-threonylcarbamoyladenine synthase {ECO:0000256|ARBA:ARBA00012156};
DE EC=2.3.1.234 {ECO:0000256|ARBA:ARBA00012156};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|ARBA:ARBA00030439};
GN ORFNames=PSEUBRA_SCAF4g04965 {ECO:0000313|EMBL:EST05845.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST05845.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000256|ARBA:ARBA00001866, ECO:0000256|HAMAP-
CC Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03180};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the TAF12 family.
CC {ECO:0000256|ARBA:ARBA00007530}.
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DR EMBL; KI545884; EST05845.1; -; Genomic_DNA.
DR RefSeq; XP_016290834.1; XM_016438346.1.
DR STRING; 1365824.V5ELC2; -.
DR GeneID; 27421039; -.
DR eggNOG; KOG1142; Eukaryota.
DR eggNOG; KOG2708; Eukaryota.
DR eggNOG; KOG2976; Eukaryota.
DR HOGENOM; CLU_002514_0_0_1; -.
DR OMA; WNIRLRL; -.
DR OrthoDB; 1098274at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.10.246.190; Autophagy protein Apg5, helix rich domain; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR048940; ATG5_HBR.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR048939; ATG5_UblA.
DR InterPro; IPR042527; Atg5_UblA_dom_sf.
DR InterPro; IPR048318; ATG5_UblB.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR11735:SF14; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR Pfam; PF20637; ATG5_HBR; 1.
DR Pfam; PF20638; ATG5_UblA; 1.
DR Pfam; PF04106; ATG5_UblB; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03180};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03180};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03180};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03180};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03180}.
FT DOMAIN 66..402
FT /note="Gcp-like"
FT /evidence="ECO:0000259|Pfam:PF00814"
FT DOMAIN 534..632
FT /note="Autophagy protein ATG5 UblA"
FT /evidence="ECO:0000259|Pfam:PF20638"
FT DOMAIN 694..750
FT /note="Autophagy protein ATG5 alpha-helical bundle region"
FT /evidence="ECO:0000259|Pfam:PF20637"
FT DOMAIN 837..929
FT /note="Autophagy protein ATG5 UblB"
FT /evidence="ECO:0000259|Pfam:PF04106"
FT DOMAIN 1550..1617
FT /note="Transcription initiation factor TFIID subunit 12"
FT /evidence="ECO:0000259|Pfam:PF03847"
FT REGION 437..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 173..177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 396
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
SQ SEQUENCE 1649 AA; 173659 MW; DBA4737C031DF97F CRC64;
MPSRTRVRKA DPLPYPSRPY LALGLEGSAN KLGAGIVLHK PFDPPSSSSS SAPSSISSRS
VGQVEILSNV RHTYVTPPGS GFQPSDTAKH HKEWIIRVIS EAVRRSGLES LADVDCICYT
KGPGMGAPLQ SVAVVARTLA LMYNKPLVGV NHCVGHIEMG RTITGAHNPV VLYVSGGNTQ
VIAYSAQKYR IFGETLDIAV GNCLDRFARV IGLSNDPSPG QNIEKEARKG SKLVPLPYTT
KGMDVSLAGI LSATEAYTRD KRFKPNPRVE HSDAAVGSLA NGEVWTGEGG GKHIVNMADE
TPARTDADVD VSQSGPSQLD ASVNTITPAD LCFSLQEHIF SMLVEITERA MAHIGSKEVL
IVGGVGSNQR LQHMMGVMAN ERGGSVFATD ERFCIDNGIM IAHAGLLSHR MGLDTSLEKN
VVRFVDDAQV DTIFKMSQPP LSGSQQRSAS AGNQPSSSSS AAPSTSLSAT TTPLLRQSSF
GAGSSGSSML PNSPHLGAGF SSTVTSPASA TFQPSSTYYP TSTPIATSSF RRLIWEGTIP
ICVSIDPADL PPGSDTTIDS TYLVVPRISY LPLIVAEVRK NLLELVLEQP ALTALNDKEL
WFEYEGQPLR WHWQIGLLYD YHTPNAARTT IAYQAASTTT TGLGSLRPED PHSTQSRSDS
GILPAAQPTK LPWNIRLRLS KPPVDRLHSN SGLESCKASF MSMIKEADFV RYGSTKKVVN
LRKQEQDTLW DGVTSHDYDL FWSIANKLVP NSRNSTFEIG SAATVRSPIT ARTLSLNIGA
GEERTPPMVQ RSLTNQPNES QASLAPSTVS TITSTSSDAP SATSGTATPT TGNAVRSIPI
RIFLPDNAPI VQEPAPPMLD DGRPNTLGAV LSALFPLLFP PPPSFSSFVS QAPPLAFALV
QGVRMPLDTE IAWLGSALVG PDGWVAVVIG LGQQPTAAQA AQYKQALIQQ QQLMRAQALA
QAQAQQQPGQ SSTQPQQQQQ PQQQAATMQT LQQLVQNNPQ GLNALLQAAR EGKMNPEQLA
QLKVFIGAHQ AQQQQQQQQQ QQQQIRPPQQ QQQMQQQVRP PQQQQGQPNL QQQQQQMAAA
LQQQLQQQQQ RNAAQNVLQQ QQQQQQVRPP QATSAPGQPQ MPQNEQALLE QFNRIAQPLR
NKVHALESAM ANPDLKPEDR QQCQNALQET RNQQANLAKQ IQLVRETFRQ QQQQQQQQQQ
QQMGQQQQQM PQVAPTPVAG ANPQQQTASP VVPAVPTAAG VPSTPAPAPA TAAAGTPKTQ
AKATPKAPAK SKAALKKEKE AKEKEEKEKK EKEAKEAKAA KGAAAKGKAG AASAVAASSA
AATASPAAAA KSSPVPGASG AATPAPGAGP GTSAPATPAA AAAPTPGAAG KPATNVPGVP
SAGAAPGVPM TAASGGATTP TAGTVGGTPV TAMSAAAASY ANVAIPPVLN VSSSTAPEPY
PNSAGPRSSM TQGLGVAPVI GTPAILSRPN PTGSGLNEQN DAALDDLLGL PPKSASNNAD
DLLSLPSTAD DSDVATAAAA TATAALSSTI TSPFAAAPAP TISTSTSMLT KRKISDLISE
LDANEKLTGA VEDLLLELAD EFIDSVTSMA CRLAKHRRGD KLEVRDVQLH LERNWNLRVP
FPGAVPIAPP RTKVGPGTSG AGAAGGSGK
//
