ID F7VPZ1_SORMK Unreviewed; 666 AA.
AC F7VPZ1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=WGS project CABT00000000 data, contig 2.3 {ECO:0000313|EMBL:CCC07569.1};
GN ORFNames=SMAC_06771 {ECO:0000313|EMBL:CCC07569.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC07569.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC07569.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC07569.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC07569.1}.
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DR EMBL; CABT02000003; CCC07569.1; -; Genomic_DNA.
DR RefSeq; XP_003344994.1; XM_003344946.1.
DR AlphaFoldDB; F7VPZ1; -.
DR STRING; 771870.F7VPZ1; -.
DR GeneID; 10802318; -.
DR KEGG; smp:SMAC_06771; -.
DR VEuPathDB; FungiDB:SMAC_06771; -.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_3_1_1; -.
DR InParanoid; F7VPZ1; -.
DR OMA; GGCKWQH; -.
DR OrthoDB; 52228at2759; -.
DR Proteomes; UP000001881; 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 CDD; cd02440; AdoMet_MTases; 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; 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; 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:UP000001881};
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 178..242
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 66..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 600
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 463
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 501
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 523
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 573
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 666 AA; 73542 MW; 95D46E520C3CA0BB CRC64;
MSATVRLLSF SRSSFIKPTT TSASIRSQLA SPNNKFSWTR SASHYTAKEF KKAFLDNDFH
KDKDNGFHKT KKDNGFHKHN HPNDKMGKRQ FNGKPGKFRK KQKKVVVASE GSPEEVLLHD
INALLETLTV ADVADEGATE APQAEVAKPE EVEKVEGEEK VEEKTEGKED KAETKPALLP
QGTEIEAEIL SLSSTGDGLA KQKGSASNHI YVVPFTVPGD VVKARVYRHV EQDGYSHADF
LEVLTPSPLR DDSRIQCKYF AKCSGCQFQM LDYSEQLKHK RSIVVKAYKN FSNLSPELVP
EILDTIGSPL QYGYRTKLTP HFDGPPGGNR RGFKKPMEEM PPIGFTPKGL RKVMDIEDCP
IATDAVRAGL TAERERMSKE FASYTRGATI LLRESTKRVP KPADGSEIPT PDLKPGVLPT
PIVTPSADGS YTDFKTCITD NNATSTEYID NFIFQNPAGS FFQNNNSILS PFTDHIRQHI
LPPPGSLPEG AKPIKNLIDA YSGSGLFTIT QSSLFPGGSI GIDIADKSID FARRNARLNG
LDESQCKFIA ADAPQLFESV SSLDADETVV VLDPPRKGCD ASFLRQLMQF APRRVVYVSC
NVHTQARDVG VLVRGRVGDT FGEAFVDPTE GEKKMSRYVI ESIRGFDFFP QTGHVEGVAI
LNRVDE
//
