Y1998_PARUW
ID Y1998_PARUW Reviewed; 383 AA.
AC Q6M9M7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Uncharacterized RNA methyltransferase pc1998;
DE EC=2.1.1.-;
GN OrderedLocusNames=pc1998;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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; BX908798; CAF24722.1; -; Genomic_DNA.
DR RefSeq; WP_011176541.1; NC_005861.1.
DR AlphaFoldDB; Q6M9M7; -.
DR SMR; Q6M9M7; -.
DR STRING; 264201.pc1998; -.
DR EnsemblBacteria; CAF24722; CAF24722; PC_RS09585.
DR KEGG; pcu:PC_RS09585; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_6_0_0; -.
DR OrthoDB; 1421660at2; -.
DR Proteomes; UP000000529; 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 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..383
FT /note="Uncharacterized RNA methyltransferase pc1998"
FT /id="PRO_0000162008"
FT ACT_SITE 341
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 246
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 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 383 AA; 44079 MW; B52D18AFC73DDC91 CRC64;
MLFPISKQAL SCPHFDSCAG CSHQLFVEPP IWREVIENFK ETLNPILHQG TLTGWRCRAK
LAVRGTKQNP IIGLFKKGSH EALNIPFCLV HHPRINQAVT MIQNWMERHQ LNPYQEHSQA
GDLRYLQFVV ERASGKVQIV FVLNFKDFSS PESQIWRKLL LELAQETTNA FWHSIWVNFN
PHATNTIFTD KWEKVWGEPY LWESFDGVKI CFQPSNFAQA NLDLFEKLLK KVKSWVREKA
KVVEFFAGVG TIGLSVAAKC SWIKCEEINP HSKECFYYAK QQLSSEISQK IMFYTGSADE
NLNLLQGADT VIVDPPRKGL SRKFIEGLTQ SSVDQLIYVS CGWDSFKKNK ETLISQGWNL
KKLEGYSLFP GSEHIELLTL FER
