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Database: UniProt
Entry: A0A1E4RKA5_9ASCO
LinkDB: A0A1E4RKA5_9ASCO
Original site: A0A1E4RKA5_9ASCO 
ID   A0A1E4RKA5_9ASCO        Unreviewed;       677 AA.
AC   A0A1E4RKA5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 4 {ECO:0000256|ARBA:ARBA00018045};
DE            EC=2.1.1.290 {ECO:0000256|ARBA:ARBA00012779};
DE            EC=2.3.1.231 {ECO:0000256|ARBA:ARBA00012155};
DE   AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase {ECO:0000256|ARBA:ARBA00030847};
DE   AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase {ECO:0000256|ARBA:ARBA00029750};
GN   ORFNames=HYPBUDRAFT_152427 {ECO:0000313|EMBL:ODV67515.1};
OS   Hyphopichia burtonii NRRL Y-1933.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX   NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV67515.1, ECO:0000313|Proteomes:UP000095085};
RN   [1] {ECO:0000313|Proteomes:UP000095085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in
CC         tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-
CC         homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119,
CC         Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
CC         Evidence={ECO:0000256|ARBA:ARBA00000401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-
CC         adenosyl-L-methionine = 7-[(3S)-(3-amino-3-
CC         methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-
CC         COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543,
CC         ChEBI:CHEBI:74275; EC=2.1.1.290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001806};
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004797}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000256|ARBA:ARBA00010703}.
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DR   EMBL; KV454540; ODV67515.1; -; Genomic_DNA.
DR   RefSeq; XP_020076582.1; XM_020221011.1.
DR   AlphaFoldDB; A0A1E4RKA5; -.
DR   STRING; 984485.A0A1E4RKA5; -.
DR   GeneID; 30995561; -.
DR   OrthoDB; 9938at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000095085; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR46529; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR   PANTHER; PTHR46529:SF1; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095085};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  77556 MW;  1B74F7F674D2E0EF CRC64;
     MKETNKSSAR DASIAAANRK KIEKDRRKKQ YDDLQVQGTN NSSIVSKRSV ELLYSTKLQP
     ELTTWFKFFV PKGKRRSPAI NRGYWIRMES IKRLVMKIIN NNPTKKINII NLGCGFDPLP
     FQLLEIYSET RDHLCFLDID YPELLDNKLE LIKKSPEVLD ILDDLQEITK EELELGMKLK
     SANYKILGCD LKNEKLYQEQ LESMCEPESV SVFIAEVSLA YMHHQDANKI IDISSKLPNS
     HFLILEQILP VDKHHSFAKK MLYHFEHLRS PLKCVEHYPK IENQRERFSQ WFHFIEIHDL
     LQNWNLLIDA DTKGKVKQIE EFDEWEEFIV FCQHYTIVHA TNQDSVSLYQ KQTIMPPPKF
     TVDPTPIEVR VDENTSLELK FAASALHHGK IIIHGGLAQT RTNQVLSYDY ITGQTTPLET
     INPPSARMCH TVTPIANGQL LMVGGRGRPH QTFADVYKLT DNAWVQMKSL PNGRSRHSAV
     SVANGNYVLI CGDGDGCEKD DIFQMYNVEQ NTWISLQQEH EVIPPVSSSS MVMTGEYTGV
     IYGGMIEDVT PEINYSIYEF EINIANHQIR LTKLDSNLQF GRIGSQSLVK ENKLYVIGGI
     LKEKPTDRFD SIITYDLIRK QFSSTDFGSD IWTHRSPTMI GFNLVTLPDQ NQACIVGGGG
     VCYSFGSSYN SIYLIKY
//
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