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Database: UniProt
Entry: A0A0Q9Q070_9ACTN
LinkDB: A0A0Q9Q070_9ACTN
Original site: A0A0Q9Q070_9ACTN 
ID   A0A0Q9Q070_9ACTN        Unreviewed;       408 AA.
AC   A0A0Q9Q070;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:KRE96081.1};
GN   ORFNames=ASG76_03275 {ECO:0000313|EMBL:KRE96081.1};
OS   Nocardioides sp. Soil774.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE96081.1, ECO:0000313|Proteomes:UP000051100};
RN   [1] {ECO:0000313|EMBL:KRE96081.1, ECO:0000313|Proteomes:UP000051100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil774 {ECO:0000313|EMBL:KRE96081.1,
RC   ECO:0000313|Proteomes:UP000051100};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE96081.1, ECO:0000313|Proteomes:UP000051100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil774 {ECO:0000313|EMBL:KRE96081.1,
RC   ECO:0000313|Proteomes:UP000051100};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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: 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:KRE96081.1}.
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DR   EMBL; LMSM01000005; KRE96081.1; -; Genomic_DNA.
DR   RefSeq; WP_056600377.1; NZ_LMSM01000005.1.
DR   AlphaFoldDB; A0A0Q9Q070; -.
DR   STRING; 1736408.ASG76_03275; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000051100; 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   CDD; cd02440; AdoMet_MTases; 1.
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; 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; 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          14..77
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        360
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   408 AA;  44085 MW;  1F80DE2DB722EE05 CRC64;
     MSRHHHRPRK ARGRSRVGER FEAEVGPVAH GGHCVARLPE PESRVVFVRH AIPGERVVVE
     ITEGTDGDRF WRGDAVSVVE ASPDRVEAPC PVAGPGLCGG CDFQHVAVPA QRALKTAVVR
     EQLVRLGRLD AGSPLVAGLE VQAVPVPGRP DDGLRWRTRQ RYAALPDGQP AMRAHRSHRL
     VPIDDCLIAA EGARPRDAVD GAVVEEGAPR PSRDILTHDV TRGETSHPFT VAADGFWQVH
     PEAPRVLVET VLELLAPQPG ERALDLYAGV GLFARFVGEV TGARVVAVEG DRSASQHARA
     NLSALEGAVV ECGPTESVLR EGYDEPFDLV VLDPPREGAK RAVVEQVVDR RPRAVAYVAC
     DPAALGRDIA IFAEHGYELT AIRAFDLFPM THHVECVALL RRVGPGQS
//
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