ID C4Y3W6_CLAL4 Unreviewed; 535 AA.
AC C4Y3W6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=TRAM domain-containing protein {ECO:0000259|Pfam:PF01938};
GN ORFNames=CLUG_02338 {ECO:0000313|EMBL:EEQ38212.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ38212.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ38212.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ38212.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408078; EEQ38212.1; -; Genomic_DNA.
DR RefSeq; XP_002616894.1; XM_002616848.1.
DR AlphaFoldDB; C4Y3W6; -.
DR STRING; 306902.C4Y3W6; -.
DR GeneID; 8498211; -.
DR KEGG; clu:CLUG_02338; -.
DR VEuPathDB; FungiDB:CLUG_02338; -.
DR HOGENOM; CLU_014689_3_2_1; -.
DR InParanoid; C4Y3W6; -.
DR OMA; FNECNGC; -.
DR OrthoDB; 52228at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA 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; 2.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR025795; tRNA_(uracil-5-)_MeTrfase.
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 Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000007703};
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 80..147
FT /note="TRAM"
FT /evidence="ECO:0000259|Pfam:PF01938"
FT ACT_SITE 485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 485
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 403
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 458
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 535 AA; 60976 MW; 2A74BD8AAEF612D7 CRC64;
MTLFSILPKQ LSNRCLQIRA ASSYASLLKK KTKRGTTDKT SRDQILHLDI TNFLREQTKT
LDHVKIPEDL IFKFLFAKKS EQVDVQEVHI LALTSEGEGL ALIPRSSYYG ESTSALYTVV
KVPKTTVGDV VTIRLRRHHE FYAEADLTNV TGKRGKNAKR NDRLVVCQHF NECNGCQIQM
ISYEDQLKFK ADVIQRAYRY FHPELKLEEL HDFGFVVPSP LQYSYRTKLT PHAKVPRSLA
KTDLPLAVGF DSIRKISPLV DIQNCPIAAP SINKTIPYLK ERFQKTLEEC LETGSKKKID
SNFLLRDSMQ IDGETGSHEY VCLTRRNNVI TEKIGEFLFQ FEANEFFQNN RSILPTFLEF
IKFHLSQIPG GYTHLIDAYC GSGFLGISLS DTLPQDGKVF GIEISKKSIA YAKHNAGING
LDRINKVQFV HGNSDSMFTD EQFLRSGVNS KDCVLLMNPS RKGSTEEFMA QLLEFKPKAI
IYISCNVFSQ ARDLATFERL QRRSSVKYKV KTITGFDFYP QTKHVETVAI LELEN
//
