ID A0A218XF84_PUNGR Unreviewed; 1019 AA.
AC A0A218XF84;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=SAM-dependent methyltransferase TRM5/TYW2-type domain-containing protein {ECO:0000259|PROSITE:PS51684};
GN ORFNames=CDL15_Pgr012929 {ECO:0000313|EMBL:OWM83448.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM83448.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC Evidence={ECO:0000256|ARBA:ARBA00001168};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWM83448.1}.
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DR EMBL; MTKT01001932; OWM83448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218XF84; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.30.1960.10; tRNA wybutosine-synthesizing-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011498; Kelch_2.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003827; tRNA_yW-synthesising.
DR InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF31; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 3 HOMOLOG; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF13964; Kelch_6; 1.
DR Pfam; PF02475; Met_10; 1.
DR Pfam; PF02676; TYW3; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF111278; SSo0622-like; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 757..1016
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 111917 MW; B4877618AF576CF2 CRC64;
MEFEKRKAAT MASLGCTETD KSPKGSLDAP IIPLLTAINS HPCFFTTSSC SGRISILSQP
SSPAPAEKKK ARGGTWLYIS HSPADPDSIL SLLFPPVPAQ PPCDLVFRFE PLILAIECRD
LDSAQFLVST AISCGFRESG ITSANGRRVI VAVRCSIRLE VPLGRSNDIA VSREYVRFLI
EVANEKMEAN RRRTDGFLQT LLQKNGFGDT PVKLVNGTGD GESLEYIEDL GKDAPLDKSD
GYSEVHDCSL SVAWLNVCGE PIEKLFLWGH SACVIDKGST KKVLVHGGFG GMGRHARRND
SLLLDPLDGT VEAIDTAGAP SPRMGHTASL IGEQMFVIGG RADPTSILSE IWALNTATNQ
WTLLNCNGDS FPPRHRHAAA VLGSRIYVFG GLNNDTIFSS IFVLDEKDLR WEELKVGGEQ
PCARHSHSMV AFGSQIFMFG GYNGEKALGD LYSFNVKTRV WRKEKALGRS PYARFSHSMF
VYKHCLGIIG GCPVKQHFQE LSLLDMHSQS WKHFSLNSVG KELFVRSTVS VVGDDLVIVG
GGASCYAFGT KFSEPMNIAL HTLAASNQFP FNCQQVQQLE NPQNLGEALG SSSEDGKGLS
ETWKSASNWY LQFERKHAKP GKDLLKKFGW LDHGRKVCSS SNGTRICFPV TEKLYILFHE
KGRVDPSIDT SHGSESNIVE LPPLKESVGQ GISLNEISSS KALNLLKQCG GTILAYETAE
FRKSVRSPSI VIKQAAASLI KQKGLPEKLL EQLPSRWERL GDIVVLPGTS FKDPLWDTIG
GELWPIIAKA LNTNRLARQG CVAPTGTRDS TLKMLVGDNG WVDHRENGIL YSFDATKCMF
SWGNLSEKLR MARLDCGDEI IVDLFAGIGY FTLSFLVRAK AKLVYACEWN PHAIEALHHN
LKANSVADRC IVLEGDNRIT APKGVADRVC LGLLPSSEGS WVTAVRVLRK EGGMLHVHGN
VKDSDENTWV EHVANSIHSI ATSEGRCWEV TIGHVERVKW YAPHIRHLVA DVRCKGNQR
//
