ID D4B3N3_ARTBC Unreviewed; 637 AA.
AC D4B3N3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=TRAM domain-containing protein {ECO:0000259|PROSITE:PS50926};
GN ORFNames=ARB_03072 {ECO:0000313|EMBL:EFE29731.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE29731.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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: 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:EFE29731.1}.
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DR EMBL; ABSU01000034; EFE29731.1; -; Genomic_DNA.
DR RefSeq; XP_003010371.1; XM_003010325.1.
DR AlphaFoldDB; D4B3N3; -.
DR STRING; 663331.D4B3N3; -.
DR GeneID; 9525723; -.
DR KEGG; abe:ARB_03072; -.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_3_1_1; -.
DR OMA; GGCKWQH; -.
DR OrthoDB; 52228at2759; -.
DR Proteomes; UP000008866; 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:0009451; P:RNA modification; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
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; 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; 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; 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; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 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:UP000008866};
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 161..229
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 90..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 584
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 584
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 441
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 489
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 510
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 557
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 637 AA; 70921 MW; 90693CEF60F7487A CRC64;
MVTNLDILVG KESLKVKLIK VKVKSVSFLR KTILQQHCFN FHSRGMFLRP LNVRITSFSR
FRALRTPATQ LTTPSVHQYS TVPRAIKIVG GFDMPGQGKA QQHKGRGREP QRKKPKKEKS
KAEGGADEVV ELDVKNLLEN NKRKSEENGE KHTDAETSVS VVHEGKKDSP FPETEVTVSE
LSSTGEGLAL SPNGDHVYIV PFALPGETAR VRIYKTIKPK SYSLTDLVEV LKPSEQRDDS
LIKCQYFGKC SGCQLQMIPY QDQLQHKKRI IEKAYANFSG LLPELIPAIG DTMGSPMQYG
YRTKLTPHFT QPARNRRQEH SSDAPEIPPI GFMMKGRRKV MDIEDCPLGT DIVRSGLKNE
RKRVAENLQQ YPYGGTLLVR ESTKRVERNK ENEALPSTDK VIRTTFPEYV EEKTYITDQN
GISVEYVEDY QFHNIAGTFF QNNNSILPSF TGYVRDNALH PEPKPDATPA ESAAAAKSNP
KLKYLLDAYC GSGLFTIVLS GTFRSSLGID VAASSIKCAR ENAKLSNVPN TGFAAADAAA
LFKDVPYPAD QTLLVIDPPR KGCDTNFLNQ LLAYGPTRVL YVSCNVHTQA RDVGVLVEGK
NGVRYDIESI RGFDFFPQTS HVESVAVLTK AIETKAE
//
