ID   A0A0G4G4D2_VITBC        Unreviewed;      1007 AA.
AC   A0A0G4G4D2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=TRAM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Vbra_22663 {ECO:0000313|EMBL:CEM22789.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM22789.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM22789.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
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DR   EMBL; CDMY01000558; CEM22789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4G4D2; -.
DR   STRING; 1169540.A0A0G4G4D2; -.
DR   VEuPathDB; CryptoDB:Vbra_22663; -.
DR   InParanoid; A0A0G4G4D2; -.
DR   OMA; FCGIGFY; -.
DR   OrthoDB; 276980at2759; -.
DR   PhylomeDB; A0A0G4G4D2; -.
DR   Proteomes; UP000041254; 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   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; 3.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000041254};
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   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          987..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..798
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         504
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         525
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         833
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   1007 AA;  112886 MW;  F930C74127396C19 CRC64;
     MIRQPASRLS SLPRPPRPCD RPPSRSFAHH RSSPKIMKMP GHTNSSTRKE YNYAGDERAN
     VVKRLDPGDV LYGMTVRHID WYGNGVVRLA VRQFRMDHDF AFPRALPGEK LALRVDDARK
     RHWKDYDISL IGTTQRSEDE VEIPCPHFLQ NCGGCAFQHY RYDKQIEQKT TLLKELFRDY
     NMPYIEDVPT GKRKKGLYVE GETNQALLID APPAHSQQHI TGGEWAALPE GDRPLQIGAP
     SSGENALLEM GSGGGEVTEV GGGAVYSGKV ERRPLSGGRR RDVTPCLLHT FIRSPKPFRF
     RNKLDFAFQH RNVPMIGLFH RQAPSVLPID ECLLAPSAIQ ETYEVCKEAF RELLANDGMT
     IYSLRTGLGI LKNLTLRYAT NLDGKTEILV NVVTGSPVDA ERLLPLVDLL SAKVPQVVGV
     VANVSRTRWG EVHTEGVLGQ GQYGRDEQLL YGRNYILQRV MGQQVFRITG SSFFHTNMLL
     VDRLCEVVLE MADPSPDDVV WDAYCGSGML GILFTKRCRH VVGVDWAPQN MKECRENMKL
     NNVPPNKMRL VLANLSNRFT LRQLALHVRR WAIEQVDPDV IESINERVRN AWLAGTKTSR
     VIERNEMGPS PFLNLPPPQP QPADTDTPSS DTDADLPPSP PPRLEWDTPS DPQYHVEMQL
     KALKLLAKEE EDEVMRAQRE AAMRVLNISD PLVGPDLTDF DAHTTEGLRK DKKPKLTPNV
     YLADSEGASR YLAEADVAIS ERKEEDELVP ATGTSDDRLL EAPDDESADD SVEAVASEAD
     DELFEDESEG DIEEEGDDSS EVTMGRREEE DAVGQPRRGG HYTIPPPDIL VLDPPKDGCH
     KVFRRWLRSL VVKKVVYVSN SPRRAIRDAQ HLILMGYQIE RVQPIDIYPH TTHFQIVMLL
     TLRDPPAPVH QPGQGPIRQA GSSQETAEER LTDGRGEGAE GRLEIAASLG LPIANPLTTQ
     SIPVKRGENV RPPTTARMYK GIRRKYRRKG GLTLASDEAP RTRHKVS
//