ID A0A1I0QDL4_9EURY Unreviewed; 415 AA.
AC A0A1I0QDL4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|HAMAP-Rule:MF_01922};
DE EC=2.5.1.114 {ECO:0000256|HAMAP-Rule:MF_01922};
DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN Name=taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN ORFNames=SAMN05216285_3423 {ECO:0000313|EMBL:SEW25135.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEW25135.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC component of the wyosine derivatives biosynthesis pathway. Catalyzes
CC the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-
CC aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of
CC tRNA(Phe). {ECO:0000256|HAMAP-Rule:MF_01922}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01922};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000256|HAMAP-Rule:MF_01922}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01922}.
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DR EMBL; FOIS01000004; SEW25135.1; -; Genomic_DNA.
DR RefSeq; WP_049990089.1; NZ_JROF01000011.1.
DR AlphaFoldDB; A0A1I0QDL4; -.
DR STRING; 1202768.SAMN05216285_3423; -.
DR eggNOG; arCOG10124; Archaea.
DR OrthoDB; 8079at2157; -.
DR Proteomes; UP000183275; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01922; TYW2_archaea; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR030867; TYW2_archaea.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922};
KW Reference proteome {ECO:0000313|Proteomes:UP000183275};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01922}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01922}.
FT DOMAIN 142..415
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
SQ SEQUENCE 415 AA; 44742 MW; BFEF5334CF6CCD0D CRC64;
MPDDPERGGE PAEPDESPDG PASDVDARLD RADAPLAAVV EKSRAETAIE SLRAEGVYDD
SRRVREARGR SGAKPSDDAI QSSTREDGPA RIALPVTDPP SETRVLEVVR QLDPEPRNTD
LEDLLADRGW SDEALESAPG SWAVIGSVIL VTVPEGCPDE ADLGEALLEL HGEADSVLAD
EGIANDGAAG TYREPRTRLI AGERDTETIH TEHGTRYGLD PAAVMFSPGN QAERARMGEV
ASADEQVFDM FAGIGYFTLP MARSGARVTA TEINPTAFRY LVENAMLNDV GDQVDAYMTD
CRDLAGEIEA DRVVMGYYGS GNESERADGD RDGGAHGTRA DEAHEFLDDA LTALVPDGVV
HYHEATPESR LWDRPLARLE SAADAADRKL EVLEKRRVKS HSAGVDHVVV DARFD
//
