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Database: UniProt
Entry: H2ZX29_LATCH
LinkDB: H2ZX29_LATCH
Original site: H2ZX29_LATCH 
ID   H2ZX29_LATCH            Unreviewed;       686 AA.
AC   H2ZX29;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   Name=LCMT2 {ECO:0000313|Ensembl:ENSLACP00000001950.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000001950.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000001950.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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; AFYH01099219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01099220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2ZX29; -.
DR   Ensembl; ENSLACT00000001964.1; ENSLACP00000001950.1; ENSLACG00000001742.2.
DR   GeneTree; ENSGT00940000162599; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000001742; Expressed in post-anal tail muscle and 5 other cell types or tissues.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:InterPro.
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; PF13854; Kelch_5; 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:UP000008672};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ   SEQUENCE   686 AA;  76458 MW;  CBA61AF0702BFCDA CRC64;
     PRNQEQISQF VQGTNDSSIV SKCSMVKLDY FKDDFLKYFV KKSSRRAPLI NRGYYIRAKA
     VDHCFKQFLM QTGGHPQIGI FIQILSLGAG FDSSYFRLKA GGLLKNVIMY EVDFPDVVSR
     KAALITNEKE LAELVGSAGE IRPAESGIVC LSGTDYRLLG VDLSELEKLD EGLIGAGLNL
     TCPTLILSEV VLTYMDNARS SAVIQWASEH FASAVFVIYE QIRPADPFGQ VMQKHFKQLN
     STLHALVEYP DREAQKKRFL DLGWEESTCV DMNEFYFGFI PKEERKRLET LEPFDEFEEW
     HLKCSHYFIL TAFKGELKIC SMLNAPTGSL LTKSVPFSSK TISASPCEVD SKVSGLRRYG
     HRSCLIKSNV VITTGGFGEQ AGQHGRLKDL QLSVKSGAIW EHGPVTVEDT EQLWDARIFH
     SMTPISDDQC VIVGGRLSPL NPSTNILCLK CRQKSDFDSC SVNVSVQEVC VDMKSLSPRW
     RHSATGMKYK DQSYLFIYGG CSPTDKVLND WYFLNLEDFS RTEILVEGFV PEGRHSHSAC
     LWNGAVVIAG GLGPEEMPLG SIYLLIPTTT GFTWQEVEAS PSVIPRYSHT AHIVDDKLLL
     VGGVLIHSDT IPGVTVIDLK TGQCVDYQIN TAHLEWPLML HNHSSVLMEE EKQLFVIGGG
     GNCFSFGTHL NQHPVLLSLA SVDEGR
//
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