ID   Y742_CHLTR              Reviewed;         396 AA.
AC   P55137; O84747;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Uncharacterized RNA methyltransferase CT_742;
DE            EC=2.1.1.-;
DE   AltName: Full=Protein HOM1;
GN   OrderedLocusNames=CT_742;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-396.
RC   STRAIN=L2;
RA   Kilani R.T., Kaul R., Meuser R.U., Tao S., Wenman W.M.;
RT   "Late developmental stage-specific protein in Chlamydia trachomatis
RT   resembles eukaryotic homeo-box.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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; AE001273; AAC68337.2; -; Genomic_DNA.
DR   EMBL; M94254; AAA91052.1; -; Genomic_DNA.
DR   PIR; H71476; H71476.
DR   RefSeq; NP_220261.1; NC_000117.1.
DR   RefSeq; WP_010725329.1; NC_000117.1.
DR   AlphaFoldDB; P55137; -.
DR   SMR; P55137; -.
DR   STRING; 813.O172_04120; -.
DR   EnsemblBacteria; AAC68337; AAC68337; CT_742.
DR   GeneID; 884537; -.
DR   KEGG; ctr:CT_742; -.
DR   PATRIC; fig|272561.5.peg.816; -.
DR   HOGENOM; CLU_014689_7_2_0; -.
DR   InParanoid; P55137; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000000431; 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:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
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.
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..396
FT                   /note="Uncharacterized RNA methyltransferase CT_742"
FT                   /id="PRO_0000161967"
FT   ACT_SITE        352
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         8
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   VARIANT         261..263
FT                   /note="AGI -> RGT (in strain: L2/434/Bu)"
FT   VARIANT         334
FT                   /note="R -> K (in strain: L2/434/Bu)"
FT   VARIANT         373
FT                   /note="R -> H (in strain: L2/434/Bu)"
SQ   SEQUENCE   396 AA;  44695 MW;  DC19DF9A9272C8C8 CRC64;
     MLSCYRNCKH FGVCGGCSSP QMEYASSLKT KELALHNLFA PLIPSQNILP VIPCSPLLRG
     RNKMEFSFYQ TVDGEKTLGF ISPSKPKKGI PITECLMIDE RAMDILNITR SWWTAHPDLS
     AYYPPLNKGS LCTITVRVGN ISNDFMIILT TSGREEFAVP LNIIQEWQQS LLDSGLPITS
     IFWEEKLSAR NSPTTFRTTH LYGAPFLKQQ LSIDGRSSLF HIRPRSFFQP QSLQAEKIIQ
     TIKEFIDPCG EETLLDLYCG AGIIGILLAP YVKKIIGVEL VPDAVASAQE NIQLNSVDME
     VFLEDAKQFC KRNENLPSPD IVVIDPPRCG MQNRALKYLL RMAPKKIVYV SCNPLTQIQE
     CSVLVEQGYQ LRRMQPIDQF PHTNHLENIV LLERLS