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Database: UniProt
Entry: I7J592_9CLOT
LinkDB: I7J592_9CLOT
Original site: I7J592_9CLOT 
ID   I7J592_9CLOT            Unreviewed;       481 AA.
AC   I7J592;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:CCJ33571.1};
GN   ORFNames=CAAU_1487 {ECO:0000313|EMBL:CCJ33571.1};
OS   Caloramator australicus RC3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Caloramator.
OX   NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ33571.1, ECO:0000313|Proteomes:UP000007652};
RN   [1] {ECO:0000313|EMBL:CCJ33571.1, ECO:0000313|Proteomes:UP000007652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC3 {ECO:0000313|EMBL:CCJ33571.1,
RC   ECO:0000313|Proteomes:UP000007652};
RX   PubMed=21421756; DOI=10.1128/JB.00193-11;
RA   Ogg C.D., Patel B.K.C.;
RT   "Draft genome sequence of Caloramator australicus strain RC3T, a
RT   thermoanaerobe from the Great Artesian Basin of Australia.";
RL   J. Bacteriol. 193:2664-2665(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:CCJ33571.1}.
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DR   EMBL; CAKP01000082; CCJ33571.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7J592; -.
DR   STRING; 857293.CAAU_1487; -.
DR   eggNOG; COG2265; Bacteria.
DR   Proteomes; UP000007652; 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   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; 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   NCBIfam; TIGR00479; rumA; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000007652};
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          28..86
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        435
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         360
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         408
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   481 AA;  54963 MW;  08A8B7C3CE7C9BCA CRC64;
     MFILYFYSDK ILKIKILKRV MKLAKYIPVE EGKIYELDIT GMGFQGEGVG RIENFAIFVK
     GALKGEKVKV EIQKVQKNFA FGKLIEIVKS SQYRTNPICP IYESCGGCQI QHMTYEGQLE
     FKRERVEDVI NRIGKITNVK IHNTIGMEKP LRYRNKVQLP VRRENGEVKI GFFKQGTHDV
     IDVRECFIQD EIADKVVNLT REWINKYNIE PYDETNGSGI VRHIMIRKAF ATGEVMVVIV
     TNGEKLPFKE EFIDLMVKNI DGLKSIVQNI NSKITNVILG EKNILLWGQD YITDYIGKFK
     FRISQLSFFQ VNPVQTNVLY NKALEYANLS GDEIVFDAYC GTGTISLFLA QRAKKVYGVE
     IVEEAIKNAR ENARENDMQN VEFIVGKSEE VIPKLIEKGI IPDVVVVDPP RKGCDERLLH
     SIAKANPKRI VYVSCDPSTL ARDLNLLEKL GYKTIEVQPV DMFPQTAHVE CVVLMQNVTN
     K
//
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