ID A0A1I6AK33_9BACI Unreviewed; 453 AA.
AC A0A1I6AK33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SFQ69034.1};
GN ORFNames=SAMN05421670_3408 {ECO:0000313|EMBL:SFQ69034.1};
OS Psychrobacillus psychrotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ69034.1, ECO:0000313|Proteomes:UP000198734};
RN [1] {ECO:0000313|Proteomes:UP000198734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
RA Varghese N., Submissions S.;
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; FOXU01000008; SFQ69034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6AK33; -.
DR STRING; 126156.SAMN05421670_3408; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000198734; 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:UP000198734};
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 4..62
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 383
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 453 AA; 50804 MW; B4154215667118BE CRC64;
MNTPVQKNDQ LTVYIEDLTH DGAGVAKVDG YPLFIAGGLP HETVEVHVLK TLKNYGFAKL
KNIVEPSPFR VEAPCPVFYE CGGCQLQHMT YEGQLAWKES MVRNVMKRIG KIDAPVLPVK
GMDKPWEYRN KSQIPFDLEN GQVIAGFYQA KSHRIADTNT CLIQSDEADR LLRAVKENAL
KLDLVPYNEE TKKGQLRHLV VRKGRATGEV MVVLVTKHAK LAKQEEIIQF IREVEPNVKS
IVHNVNNQNT NVIFGNETNV IWGKAVIEDL IGDVRFEISA RSFYQVNPVQ TEVLYKQALD
YAQLTGEETV IDAYCGIGTI SLFLAQKAKQ VLGVEIVPQA IEDAKRNAEL NGFTNTYFEA
GPAEEVIPNW YKEGKHADVL VVDPPRKGCD EALLTTIIEQ RPKRVVYVSC NPATLARDLR
ILEDGGYKTK EVQPVDMFPQ STHVECCALL ELV
//