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Y1496_BRUME
ID   Y1496_BRUME             Reviewed;         415 AA.
AC   Q8YFM4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Uncharacterized RNA methyltransferase BMEI1496;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BMEI1496;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52677.1; -; Genomic_DNA.
DR   PIR; AB3439; AB3439.
DR   RefSeq; WP_004683080.1; NZ_GG703778.1.
DR   AlphaFoldDB; Q8YFM4; -.
DR   SMR; Q8YFM4; -.
DR   STRING; 224914.BMEI1496; -.
DR   EnsemblBacteria; AAL52677; AAL52677; BMEI1496.
DR   GeneID; 29594350; -.
DR   KEGG; bme:BMEI1496; -.
DR   PATRIC; fig|224914.52.peg.2095; -.
DR   eggNOG; COG2265; Bacteria.
DR   OMA; FYAGDMK; -.
DR   PhylomeDB; Q8YFM4; -.
DR   Proteomes; UP000000419; Chromosome I.
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; 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.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..415
FT                   /note="Uncharacterized RNA methyltransferase BMEI1496"
FT                   /id="PRO_0000161960"
FT   ACT_SITE        370
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         276
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   415 AA;  45001 MW;  159A502714DFA177 CRC64;
     MTSSKTGQIT IRSIGAGGDG VANLPDGQIY VPFTLPGEVV NVARDKNRAT LMALLEASPE
     RQNPACRHFE DCGGCALQHW QDEPYRLWKR ELVVGALKGR GTDVEVAPLV ACNPHTRRRA
     VFAARKTEKG VLLGFNRHQS HEIIDIVECP VTVPEIIARL DDLREVGALL APGSGPFKLA
     ATLTESGLDL AASGCGKLND EQRRALTALV IKKDFARLSH EGEIIVEPKK PLIHFGKVPV
     PIPPGCFLQA TAEAEETMAA LVLAHLGKAR RVADLFCGVG TFALRIAEKS AVHAVENDAA
     ALAALDRGVR HVQGLKPVSI ERRDLFRRPL MTKELLPYNA VVFDPPRAGA EEQALELAKS
     KVEKVVAISC NPVTLARDLA ILQKGGYRIE RVTPIDQFLW SAHVEAVAVL TKGRQ
 
 
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