ID A0A0D2HQN7_9EURO Unreviewed; 1141 AA.
AC A0A0D2HQN7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=Z520_00863 {ECO:0000313|EMBL:KIY04171.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY04171.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY04171.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY04171.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN848062; KIY04171.1; -; Genomic_DNA.
DR RefSeq; XP_016638293.1; XM_016771383.1.
DR AlphaFoldDB; A0A0D2HQN7; -.
DR STRING; 1442371.A0A0D2HQN7; -.
DR GeneID; 27706609; -.
DR VEuPathDB; FungiDB:Z520_00863; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000053411; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 846..1011
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 972..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 126557 MW; 6A2D899D2777482C CRC64;
MSPQEGNAND EIPMEKNAGL VMGTNNSSIV SKRSVERLYL PQPHFYRYFV KKPIRRSPTI
NRGYWLRMRA IDWVVRQFLE KPSDLNKVII NLGCGYDPLP FQWMAQHPDL CGNTKFIDVD
FEELMISKRE IILNTPKMSE MLSTTPDRGS MKGVVLDSDV YVAIGCDLRN PPRLERLLRS
VVDIDQCLVL CVAEVSITYM ATKDADALIA WTSTLSPDVT FCLLEQQSPD RPDNPFTAAM
LKHFAKLGTP LRSVLTYPGC HTQTLRFQDA GFPHVEMQNL WELWADPRFL SPSQRISLDE
VEPFDEWEEF ALFASHYCLV IAQTGPEPLV PEQQRSRRAS VDSLASDMSA RTVSPHRDNT
QWFAYKYSAN PEQEGRTHHG SAFIVPGQDA IAVHGGVGLR GRLSTTSVYT STDSTLPYPS
APPEDIGARC CHTITTLSNG QNLLVGGRGS PSSPMKDCWL QTDSKWERVH DLPEPRFRHR
AAAVVLPYDQ YGVVVFGGKT SATRIAIDCL LWDKENGWQV LRSLKQDPMP RFGASFVRLG
FNHGLLLGGM RQDGVICQGL WKWRLIIRDN KVMGINFRVS TALDASAGIW PWMNRLGASY
SVIRDELLLI GGVAKHGCIP KDYEILSIVG SFSAFNDYEK EMDFRVACVL PKRDPNVPRP
FLIGHSTHYT ARQTTLIVGG GATCFSFGAY WNPGCWLLYD REAGLSSHWT MVKPETRKLA
PQSTPQGGAP TARISTPIEH IKIETEQDFT RVLSEGRPKL FSDLDIGQCT STWTAAYLLS
KIPPSKSVVV HSAPGRTMNF QRKDFAYKTT SFHEFIHQLD SDPNAHMYLR SISSTNPTLS
PADFASDWPE LAPDFAVPRE LSFVVRNQHS SPLRISANVN MWLHYDVMAN VLFQIRGTRK
LILFPPGDLK HLSFPPGSTT SSIDIFESTQ QSGEGGEDTV RVVPGTKPHI AILQPGDALY
IPPLWAHTGT PLPAGAPRKA QQPVSLSTSE IASTSTSTST STSAAAAAAT AASQPTPESP
STTTNPSTAE DRINISVNIF FRTLHSTKYA AGRDVYGNRD LAAYEDGRRD VERIVRRFLK
VDTAEGPESS SGTGTGTATE TETSTGGTPT TGLDTGVIPR DIVRAYLERL ADELRQRAEK
L
//
