ID   Y053_NANEQ              Reviewed;         447 AA.
AC   Q74N58;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Uncharacterized RNA methyltransferase NEQ053;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=NEQ053;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(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; AE017199; AAR38908.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74N58; -.
DR   SMR; Q74N58; -.
DR   STRING; 228908.NEQ053; -.
DR   EnsemblBacteria; AAR38908; AAR38908; NEQ053.
DR   KEGG; neq:NEQ053; -.
DR   PATRIC; fig|228908.8.peg.53; -.
DR   HOGENOM; CLU_014689_8_1_2; -.
DR   OMA; FYAGDMK; -.
DR   BioCyc; NEQU228908:GJB6-57-MON; -.
DR   Proteomes; UP000000578; 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:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 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..447
FT                   /note="Uncharacterized RNA methyltransferase NEQ053"
FT                   /id="PRO_0000162052"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
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"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   447 AA;  52472 MW;  98F000447B5377EC CRC64;
     MFTKYKFLYF LFDSTFFKYW YVIPMAMKIY IEGFDEKGYG VGNNIHVPFA YPGDIVEVKV
     RRKGKKKIGE IVKIIEESPY RTSNKYCAHL GKCGGCLWGL MDYQYQLEFK KKVIENLFGY
     DKDIIPSPKT IYYRNRMDYP IYNKVSLKEP GKWYGYIPIK ECKMLSKEAE IIINEFNKFI
     EKYKIPSWDT VKHTGFLRYL VIREGKFTKE RMIHIITYKR KKFEELWDFI ENIKDLVTSV
     YWGIREDLGD VSISEKLYHY YGSKFLRERI LDIEYYISPN SFFQTNSYQA VNLVKIVKEF
     LEPSENDVVL DLYSGVGLFS LQIANEVKKV IGIEIVEEAV EMAKLNASIN NIDAEFIASP
     VEKAPIIKAN KIIVDPPRAG LTNKAIEYIE KINPDTIVYV SCNPYTQKRD INKLKGYKII
     DMQPLDMFPN TPHIENVILM KKSRTTD