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Database: UniProt
Entry: U4LK46_PYROM
LinkDB: U4LK46_PYROM
Original site: U4LK46_PYROM 
ID   U4LK46_PYROM            Unreviewed;      1065 AA.
AC   U4LK46;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=Leucine carboxyl methyltransferase 2 {ECO:0000256|ARBA:ARBA00030231};
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=PCON_13237 {ECO:0000313|EMBL:CCX32474.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX32474.1};
RN   [1] {ECO:0000313|EMBL:CCX32474.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX32474.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX32474.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC       that acts as a component of the wybutosine biosynthesis pathway.
CC       Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC       the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC       tRNA. May methylate the carboxyl group of leucine residues to form
CC       alpha-leucine ester residues. {ECO:0000256|ARBA:ARBA00025588}.
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; HF935878; CCX32474.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4LK46; -.
DR   STRING; 1076935.U4LK46; -.
DR   eggNOG; KOG2508; Eukaryota.
DR   eggNOG; KOG2918; Eukaryota.
DR   OMA; WEVDFPD; -.
DR   OrthoDB; 9938at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000018144; 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; 2.60.120.650; Cupin; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR003347; JmjC_dom.
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; PF13621; Cupin_8; 1.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF04072; LCM; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CCX32474.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCX32474.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          899..1050
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  118496 MW;  97B5CB0F58C403B6 CRC64;
     MSSPDVDTEP KSDTQHQQTA PTQQNQQTSP PPPPPTTNGT LQDAAATPAA TPATATNPNP
     NAKGKPKISE KAKLDAAVIG TNNSSITSKR SVERLYSHED EQQFLRYFVK KPQRRSPILM
     QAVEYVVHSF LQEELPHLSM RQKKVVVNLG CGYDPLPFQC LAKEKPNAEV LYVDIDYPDL
     ITIKAGIIAQ TPGLNGLLTD KQHHETPVDH VHYQSNEYIA LGCDLRDLDT LQRLFEKHGL
     VDHAVFFTAE VSLTYMAKDS VDALIAWAAS LPDARFSILE QIMPDGPHHP FARTMLKHFN
     ALNTPLKSIS AYPRLEDQVK RYSSRGWKSV DACDLLAFWS NRIPQSEKER IDAIPGEPFD
     EFEEFFIFCQ HYFILCAHNI SNPHTPFNGP GLSWNAGGAY HRYPSSSNHG PYPGINMTGN
     KEKTLVAEYT PSPHLKRRFG AAAATGKDSF IYHGGQGQTT RLGSALCITH SAEGIQLDKQ
     TSPSARVCHT MTTMPNGKIL LVGGRTSPDK PVADTWLLEG GVWRRVQDLP VARYRHTAAV
     PGYQNTGGNQ VLIYGGRGGN RSVLGDFWLW CEEKGWREVM IQPIGSGSQR PPPRFATSMC
     WTDRKYGAMG GGLDAKGNVL DDFWRLELHQ DPETGSETIK ALWSMVNMIA SKNLWKRFGG
     QMVYAGNGSI LYVGGVSGRG LMRREDEILQ VCCNKVVVKG VRAAFPQENA PFLVGHSVVV
     LQDRVIISGG GGVCFSMGSC TNDGIWSITN EEMCDSWRFI EEGYAPDDVD VPMPDSPAPY
     TPDQDNATNE TIECKPLPRV TISTPEEFSR IVSEGLPVVL ENLTLGPCLN KWIPSYLSTM
     IGDEKIVVHM SKSSAMSFQQ KNFKYIPMAF NDFITSAFPL TESPNNARIY FRSLSQSKPR
     DKPTRLSDDF PQIAADFILP ATLKMVSENI HSSPLRISSA DVGMWLHYDG MANVLCHISG
     RKLFRLYPPR DVSRLSFPHG ETTSTIPDIF AKYIPGTTPY EVELGKGDVV YIPPLWLHAA
     KPLTPCVAVN VFLGIWDRML MLLGRMFMRQ EIFKRMKRGG RCWRG
//
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