ID A0A197JU74_9FUNG Unreviewed; 637 AA.
AC A0A197JU74;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00012265};
DE EC=2.5.1.114 {ECO:0000256|ARBA:ARBA00012265};
DE AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00031315};
GN ORFNames=K457DRAFT_139106 {ECO:0000313|EMBL:OAQ27986.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ27986.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ27986.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ27986.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC component of the wybutosine biosynthesis pathway. Wybutosine is a hyper
CC modified guanosine with a tricyclic base found at the 3'-position
CC adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes
CC the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14)
CC to produce wybutosine-86. {ECO:0000256|ARBA:ARBA00037786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC ChEBI:CHEBI:73550; EC=2.5.1.114;
CC Evidence={ECO:0000256|ARBA:ARBA00036405};
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DR EMBL; KV442052; OAQ27986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JU74; -.
DR STRING; 1314771.A0A197JU74; -.
DR OrthoDB; 122704at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..632
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT REGION 321..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71228 MW; B1175280A98926BA CRC64;
MSSTTTSIPV LLVPGHLTKH LKVFLDKAAW RDKTKLITRY SQITSDHSAT TTSTGSTAGV
RKDSHNGCDL TQYMAMALLP VGPFSQPPTA TTTTDIRSLW DLAQDPSSPP STDLSSIDWP
APLSDPTLQK TIFLTWLLPT AFPSPKHLLV QTPLEKLQQT TSEFLLPYLQ LWAATFDPDQ
QGQQQQQGHL GPEILPELIA SLPQKWEHYS DFTFLPPTAF LAAPWPAVLK RLIALDHQQQ
HAGCASGDNG IMARWEKLVQ DALGSTHIAR KAIIPVQDIL RRPKIRPLAG DWKLHNRYKS
WIEAEEGVEE GETLETNLVE HQEMSSDLSS SKANAITNNT SGAGAESTGL YESTTSSTTT
DSDVLPTPSN FLQTYWSETC QNQVFYTWSP MFTMFSAGNI TEKERVAKSR PIFDARNKVV
VDLYAGIGYF ALVYLVHAGA KVVHACEWNP WSVEGLVRGS GRNGIPWKRY HGENVRIKSK
EEKGELQEQP FTSGQPTHRR PPHKPITTTT ATKKQKDYGQ LVVYPGDNAQ WIEYFENTAH
HVNLGLIPTA EPGWVLGVRA LCPLEGGYLH VHHNIRVGEE ESFKLYLLQS LRDLFAVWKH
SGEWSIEIRH MENVKSFAPL VFHYVVDVEC RPPTISS
//
