位置:首页 > 蛋白库 > RLMD_ACIB3
RLMD_ACIB3
ID   RLMD_ACIB3              Reviewed;         463 AA.
AC   B7H018;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000255|HAMAP-Rule:MF_01010};
DE            EC=2.1.1.190 {ECO:0000255|HAMAP-Rule:MF_01010};
DE   AltName: Full=23S rRNA(m5U1939)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01010};
GN   Name=rlmD {ECO:0000255|HAMAP-Rule:MF_01010}; Synonyms=rumA;
GN   OrderedLocusNames=ABBFA_002982;
OS   Acinetobacter baumannii (strain AB307-0294).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=557600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB307-0294;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939
CC       (m5U1939) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-
CC         methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42908, Rhea:RHEA-COMP:10278, Rhea:RHEA-COMP:10279,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.190;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01010};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01010}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001172; ACJ56212.1; -; Genomic_DNA.
DR   RefSeq; WP_000813076.1; NZ_CP001172.1.
DR   AlphaFoldDB; B7H018; -.
DR   SMR; B7H018; -.
DR   HOGENOM; CLU_014689_8_2_6; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000006924; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01010; 23SrRNA_methyltr_RlmD; 1.
DR   InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
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; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..463
FT                   /note="23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD"
FT                   /id="PRO_1000200835"
FT   DOMAIN          6..76
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   ACT_SITE        415
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         90
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         99
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         178
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         368
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
FT   BINDING         389
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01010"
SQ   SEQUENCE   463 AA;  52486 MW;  CBDDA32599B2243A CRC64;
     MKQQAKSRKP QQPEYIFQVE TLSHEGRGIA HYGSHPDHPA DKHGKKVFIR YALPGETVKA
     QITHEAKRLE EAEMVELLAE PSANRVEAVC PHYGICGGCS MQHIHPDEQI HLKQNVLQSH
     LQHFAGIQPE QWLEPIRSLQ SDYRRRARIG VRYLPKQDRL ILGFREHHSN RLTSIHTCSV
     LDKKLSDNLP ELRNLLQSLK GKAHIGHVEL AKGDHEISLL VRHIEKLNNA DVNQLRQFAL
     HKGWQLYLQP KGPESLRRID EEQGAMRLHY ALNAFDVNFA FSPLDFTQVN ATVNEQMVQL
     ACELLQLQQG ERVLDLFCGL GNFSLPLARC VGAKGQVVGV EASEEMVQRA TDNAKRNNLV
     QASFFSQDLT KDFSHHSWAN QGFDALLIDP PRAGAYEIMQ YVPNFGAKRI VYVSCNPATL
     ARDAGVLVQH GYQLKKAAVM DMFTHTEHVE SIALFEKIQE IND
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024