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Database: UniProt
Entry: A0A1S1RBC4_9ACTN
LinkDB: A0A1S1RBC4_9ACTN
Original site: A0A1S1RBC4_9ACTN 
ID   A0A1S1RBC4_9ACTN        Unreviewed;       458 AA.
AC   A0A1S1RBC4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Deoxyribonuclease {ECO:0000313|EMBL:OHV43306.1};
GN   ORFNames=CC117_11730 {ECO:0000313|EMBL:OHV43306.1};
OS   Parafrankia colletiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV43306.1, ECO:0000313|Proteomes:UP000179627};
RN   [1] {ECO:0000313|Proteomes:UP000179627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA   Hurst S.;
RT   "Sequence Frankia sp. strain CcI1.17.";
RL   Submitted (JUL-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}.
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:OHV43306.1}.
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DR   EMBL; MBLM01000036; OHV43306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S1RBC4; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000179627; 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   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; 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:UP000179627};
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          1..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          221..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        404
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         377
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   458 AA;  48205 MW;  3C7C16A5979E01DE CRC64;
     MPPSELVELE VGAVAHHGLC VARADGRVVF VRHALPGERV RARITDVSHD RYWRADAVEV
     LVASPDRVEP PCPHARPGLC GGCDWQHASL DAQRRLKARV VEESLRRIAG LDLTVLVEAL
     TSAAPDGLGW RTRMRFSRTP DGGVGLRAHR SHGVVATPDC RIADPLLASV IADPSFLQGP
     ASPDRTGQAV ELVAMPASPP DRESGAVAYS TRSGRWQVVQ VPSGEGGAEP DSRHPDSRHP
     DGPRSDGPPP PEAEVQVVET VEGRRFHLEP GVFWQVHPAA AATLVAAVRD AAGAAPGDTA
     LDLYSGAGLF AAFLAAAVGP TGQVIAVESD EAAVRSAARS LADLPWVSLR ALRVTPATVS
     RLTGGSARPG VDVAVLDPPR TGAGREVMTA LLAHRPRRVV YVACDPAALG RDVAVAAGEG
     YRLTGLRAFD IFPMTSHVEC VAILEPTSAH DQTQAAGR
//
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