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Database: UniProt
Entry: A8L0L4_FRASN
LinkDB: A8L0L4_FRASN
Original site: A8L0L4_FRASN 
ID   A8L0L4_FRASN            Unreviewed;       517 AA.
AC   A8L0L4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Deoxyribonuclease/rho motif-related TRAM {ECO:0000313|EMBL:ABW14547.1};
GN   ORFNames=Franean1_5189 {ECO:0000313|EMBL:ABW14547.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW14547.1};
RN   [1] {ECO:0000313|EMBL:ABW14547.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW14547.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) 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; CP000820; ABW14547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8L0L4; -.
DR   STRING; 298653.Franean1_5189; -.
DR   KEGG; fre:Franean1_5189; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_11; -.
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   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; 2.
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          6..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          250..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        452
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         304
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"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         425
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   517 AA;  53490 MW;  BF733A16A29FD056 CRC64;
     MTRPVPVPPS ELVELDVGPV AHRGLCVARA GGRVVFVRHA LPGERVRVRI TDVSHDRYWR
     ADAVEILVAS PDRVAAPCPH ARPGGCGGCD WQHATPAAQR RLKARVVEDA LRRLAGLDRA
     VLVEALPSEG PDGLGWRTRM RFSRTSDGGV GLRAHRSHEV VPTPDCKIAH PLLARVIADP
     VFLTGDGSPE VTGQAVELVA MPGDAVAYST RSGGWRVTET GPAAADAEGT GATRVDGATR
     VDGATRVDGA TRVDGADGAD PDSALRASAV PVRTGPDRGE PAPVEVVETV EGREFRLEPG
     VFWQVHPAAA ATLVAAVREA AAAAAGDTAL DLYCGAGLFA AFLAEAVGPT GRVIALESDE
     AAVRSAARSL ADLPWVSLRS LRVTPATVRG LVGAADQPAA PADGLPAGGA TPGPARRAVD
     VAVLDPPRTG TGREVMTELL AHRPRRVVYV ACDPAALARD VAVAAGEGYR LTELRAFDLF
     PMTSHVECVA TLEPAPAGAT GSAEPARPGT GSTALPR
//
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