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Database: UniProt
Entry: A0A1H0K2K1_9ACTN
LinkDB: A0A1H0K2K1_9ACTN
Original site: A0A1H0K2K1_9ACTN 
ID   A0A1H0K2K1_9ACTN        Unreviewed;       438 AA.
AC   A0A1H0K2K1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SDO50094.1};
GN   ORFNames=SAMN05428965_4228 {ECO:0000313|EMBL:SDO50094.1};
OS   Geodermatophilus sp. DSM 45219.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDO50094.1, ECO:0000313|Proteomes:UP000198730};
RN   [1] {ECO:0000313|EMBL:SDO50094.1, ECO:0000313|Proteomes:UP000198730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45219 {ECO:0000313|EMBL:SDO50094.1,
RC   ECO:0000313|Proteomes:UP000198730};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNIQ01000006; SDO50094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0K2K1; -.
DR   STRING; 1881103.SAMN05428965_4228; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000198730; 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:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
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; 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; 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; 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};
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          16..75
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         366
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   438 AA;  45982 MW;  EB5502C0377A0C1F CRC64;
     MAERRRRPAA HPDRGGGWTG REFEVTVGPV AHGGHCVARH EGRVVFVRHT LPGERVVVRV
     TEDRQPGFCR ADAVEVLEAA PDRVPRPCPY SGPGRCGGCD WQHVRHEGQL RLKAAVVREQ
     LTRLAGLSDD DALVRDLAVE ALPGGPLRWR TRARFAVDRA GAPGLRRHRS HDLVVLDDCP
     ITVEPAARAV LDRRWHGAGA VDVAVDSAGT VTTTRLDRRG RPQSTRVTRA GEDGRGWDDG
     TEPAGRAARS AAGRDWEVEG TGFWQVHPAA ADALTEAVAG FAAVRAGETV LDLYAGAGLF
     GGVLAPAAGD RGRVVCVEAD EAACAAAEVN LAALPQAEVW QGEVDAEGLT ELLAELGGAP
     DVVVLDPPRA GAGAAVSRVL AGAGPRAVVY VACDPASLAR DVAAFAGGGY RLAGLRGFDA
     FPMTAHVECV ALLVRAPS
//
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