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Database: UniProt
Entry: A0A0T1SKT6_9ACTN
LinkDB: A0A0T1SKT6_9ACTN
Original site: A0A0T1SKT6_9ACTN 
ID   A0A0T1SKT6_9ACTN        Unreviewed;       442 AA.
AC   A0A0T1SKT6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KQX55388.1};
GN   ORFNames=ASD33_31685 {ECO:0000313|EMBL:KQX55388.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX55388.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX55388.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX55388.1,
RC   ECO:0000313|Proteomes:UP000051136};
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:KQX55388.1}.
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DR   EMBL; LMEP01000007; KQX55388.1; -; Genomic_DNA.
DR   RefSeq; WP_056557583.1; NZ_LMEP01000007.1.
DR   AlphaFoldDB; A0A0T1SKT6; -.
DR   STRING; 1736450.ASD33_31685; -.
DR   Proteomes; UP000051136; 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; 1.
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; PF01135; PCMT; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051136};
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          7..68
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         271
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         368
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   442 AA;  47673 MW;  6A5AEB85FFCF0712 CRC64;
     MQNTPVTSLV GAEYEVEVGP VAHGGHCIAR TEAGRVLFVR HALPGERVRA RVTEGEETSR
     FLRADAIEIL DASKDRVAAP CPFAGPGKCG GCDWQHAKPG AQRRLKGEVI AEQLQRLAGL
     TPEEAGWDGT VMPAEGDKLP AGEVPQWRTR VQYAVDPEGH AGLRKHRSHE VEIIDHCMIA
     AAGVSELGIE KRTWEGMASV EAIAASGSND RQVILTPRPG ARLPLVELDK PVSVMRVDEK
     DGGVHRVHGR AFVRERADER TYRVGSGGFW QVHPKAAQTL MLAVMQGLTP RKGDTALDLY
     CGVGLFAGAL ADRVGDKGAV LGIESGKRAV EDARHNLADF PRVRIEQGKV ESVLPRTGIT
     DVDLIVLDPP RAGAGKQTVT HLSGLGARRI AYVACDPAAL ARDIAYFAEG GYKVRTLRAF
     DLFPMTHHVE CVAILEPVKK DA
//
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