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Database: UniProt
Entry: A0A067L0S6_JATCU
LinkDB: A0A067L0S6_JATCU
Original site: A0A067L0S6_JATCU 
ID   A0A067L0S6_JATCU        Unreviewed;       571 AA.
AC   A0A067L0S6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=TRAM domain-containing protein {ECO:0000259|PROSITE:PS50926};
GN   ORFNames=JCGZ_24817 {ECO:0000313|EMBL:KDP40818.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP40818.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP40818.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP40818.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; KK914327; KDP40818.1; -; Genomic_DNA.
DR   RefSeq; XP_012069041.1; XM_012213651.1.
DR   AlphaFoldDB; A0A067L0S6; -.
DR   STRING; 180498.A0A067L0S6; -.
DR   GeneID; 105631510; -.
DR   KEGG; jcu:105631510; -.
DR   OrthoDB; 120922at2759; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          84..144
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          29..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        520
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         393
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         424
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         445
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         493
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   571 AA;  63617 MW;  40D7E5C9FB48D309 CRC64;
     MTMPTNTLRH LPATHLWLHR LNKLQKLHSS ASLSPSPFTQ DPQQQRQQER TQKTQQTRLS
     NSDKNIKNDI VESIGVNNNS NSFFPKRGQT LELVCESLAF KGKGVCKVPD TGFVLMCDRA
     LPGERFIGRV TRRKGSYAEV TKVKTLSPHL DIVDAPCEYA AYCGGCKTQN LVYEAQLKAK
     EQQVHGLVVN VGKFSDKDPE FYSIMKPIVP CDFQFHYRNK MEFSFGPQKW LPKELIGEKQ
     EGSESYALGL HAPGFFDKVL NVDGCLLQSE PANTVLATVQ DCWRDSVGLT PYNVYSHAGF
     LKHLMLRTGR NAESGSLELM VNFVTSSYKP ELLKPLMEKI SAIPEVVSIM NNVNSSVGNT
     SVGEEEYTLY GKSTITEVLR GLTFQISANS FFQTNTHQAE VLYKLIEDCA GLRGDGSEIV
     LDLFCGTGTI GLTLARGAKH VYGYEVVPQA ISDAFRNAEL NGITNATFVQ GDLNKIGENF
     GNNFPKPDVV ISDPNRPGMH MKLIKFLLKL KAPRIVYVSC NPATCARDLD YLCHGVKEQN
     IKGCYKLKSL QPVDMFPHTP HIECVCLLEL C
//
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