ID   Y1179_ZYMMO             Reviewed;         397 AA.
AC   Q9X3W2; Q5NNA7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Uncharacterized RNA methyltransferase ZMO1179;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=ZMO1179;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee H.J., Kang H.S.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV89803.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF088896; AAD21539.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89803.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_017466424.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9X3W2; -.
DR   SMR; Q9X3W2; -.
DR   STRING; 264203.ZMO1179; -.
DR   EnsemblBacteria; AAV89803; AAV89803; ZMO1179.
DR   GeneID; 58026951; -.
DR   KEGG; zmo:ZMO1179; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_0_5; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000001173; 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; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
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; 1.
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..397
FT                   /note="Uncharacterized RNA methyltransferase ZMO1179"
FT                   /id="PRO_0000162051"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         47
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   CONFLICT        136
FT                   /note="K -> I (in Ref. 1; AAD21539)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  44008 MW;  4AF7DA1AB3483462 CRC64;
     MKKIIRLASK GDGVTEDGQF VPNSVPDDYI SDDGKLEFGA HHIEPVCRHF SVCGGCRLQY
     ADEEVYKNFL TDRIAEAFHQ QALSAPVLKT AHLSPPYSRR RVALRAFKAG KKLTLGYNKT
     SSHQLVDIVE CPLLDKNLFK AAMDLRSFLQ KWLAPRSLAQ IEMTLADQGI DCLLVMPFPE
     TLEATEAITA FAAEKGFARL SIDQGYGVET RWESERVTVT LGAVPVTLPA HAFLQATKDG
     EQTLVHMVKE AVGDAHFVAD LFSGLGTFAL SFEKDKRVYA AEGMRDAVLA LKQAAALAGK
     AVFVEHRDLF RRPLQKDELV RFECIILDPP RAGAKEQIAN LAILPNGRIV YVSCNPATFA
     RDAKTLLEAG WVLHWVKPVG QFPWSLHVEM VGLFTKM