ID   Y1857_NITEU             Reviewed;         393 AA.
AC   Q82TM7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Uncharacterized RNA methyltransferase NE1857;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=NE1857;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; AL954747; CAD85768.1; -; Genomic_DNA.
DR   RefSeq; WP_011112395.1; NC_004757.1.
DR   AlphaFoldDB; Q82TM7; -.
DR   SMR; Q82TM7; -.
DR   STRING; 228410.NE1857; -.
DR   EnsemblBacteria; CAD85768; CAD85768; NE1857.
DR   KEGG; neu:NE1857; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_1_4; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 1421660at2; -.
DR   PhylomeDB; Q82TM7; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 2.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..393
FT                   /note="Uncharacterized RNA methyltransferase NE1857"
FT                   /id="PRO_0000162004"
FT   ACT_SITE        340
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         72
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   393 AA;  44854 MW;  E1B2FA78B3C0E875 CRC64;
     MSFQGEITHL SQKGLGVVQH PENGLSYFVA GTWPGDRGEF EITDRALNNR KYGYARLIRL
     IQSSRHRKTP ECRFLGFSGN DCSGCPWMIA DYDSQLEQKK NRFLYAMHRV GFDLADLNIG
     AVQPSPDLFG YRNRFQVKTD GEKLGFVAEG SHHIVPIEDC LILNPACRQH LQTLRKHLPS
     REWSPAPGDD WNFIDLDDQS PAEPVLLNWK QPFRQGNDAQ NQWMRSWLKY ALEQHGHSHK
     IVELFCGSGN FTEVIAQTGC PEILAYEADP QAITVLRQKN LPGVDARTAD LYHPFIWKIL
     KKNVQDAGIL VLDPPRSGLK TLRGFFDAFA ALETICYISC DPVTFARDAW IFCKNGWKFT
     DIQLIDLFPH TPHIEITATF HKQWGNTKKG NKR