(data stored in ACNUC7421 zone)

HOGENOM: ECO5T_1_PE1011

ID   ECO5T_1_PE1011                       STANDARD;      PRT;   702 AA.
AC   ECO5T_1_PE1011; C6UNL4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase L; EC=2.1.1
DE   173;AltName: Full=23S rRNA m2G2445 methyltransferase;AltName: Full=rRNA
DE   (ECO5T_1.PE1011) (guanine-N(2)-)-methyltransferase RlmL; .
GN   Name=rlmL; OrderedLocusNames=ECSP_1054;
OS   ESCHERICHIA COLI O157:H7 STR. TW14359.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=544404;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECO5T_1.PE1011.
CC       Escherichia coli O157:H7 str. TW14359, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6UNL4_ECO5T
CC   -!- FUNCTION: Specifically methylates the guanosine in position 2445
CC       (m2G2445) of 23S rRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(2445) in
CC       23S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanosine(2445)
CC       in 23S rRNA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmL
CC       family.
CC   -!- SIMILARITY: Contains 1 THUMP domain.
CC   -!- GENE_FAMILY: HOG000218371 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6UNL4; -.
DR   EMBL; CP001368; ACT70909.1; -; Genomic_DNA.
DR   RefSeq; YP_003076985.1; NC_013008.1.
DR   ProteinModelPortal; C6UNL4; -.
DR   SMR; C6UNL4; 1-370, 390-696.
DR   STRING; C6UNL4; -.
DR   EnsemblBacteria; EBESCT00000166133; EBESCP00000155234; EBESCG00000166790.
DR   GeneID; 8215620; -.
DR   GenomeReviews; CP001368_GR; ECSP_1054.
DR   KEGG; etw:ECSP_1054; -.
DR   GeneTree; EBGT00050000009453; -.
DR   OMA; YRIYDAD; -.
DR   ProtClustDB; PRK11783; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:HAMAP.
DR   HAMAP; MF_01858; 23SrRNA_methyltr_L; 1; -.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR002296; N12N6_MeTrfase.
DR   InterPro; IPR000241; RNA_methylase.
DR   InterPro; IPR017244; S-Ado-dep_RNA_MeTrfase_bac.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR004114; THUMP.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SMART; SM00981; THUMP; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51165; THUMP; 1.
DR   PROSITE; PS01261; UPF0020; 1.
DR   HOGENOMDNA; ECO5T_1.PE1011; -.
KW   23S rRNA m(2)G2445 methyltransferase;
KW   Complete proteome; Cytoplasm; Methyltransferase; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
SQ   SEQUENCE   702 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNSLFASTAR GLEELLKTEL ENLGAVECQV VQGGVHFKGD TRLVYQSLMW SRLASRIMLP
     LGECKVYSDL DLYLGVQAIN WTEMFNPGAT FAVHFSGLND TIRNSQYGAM KVKDAIVDAF
     TRKNLPRPNV DRDAPDIRVN VWLHKETASI ALDLSGDGLH LRGYRDRAGI APIKETLAAA
     IVMRSGWQPG TPLLDPMCGS GTLLIEAAML ATDRAPGLHR GRWGFSGWAQ HDEAIWQEVK
     AEAQTRARKG LAEYSSHFYG SDSDARVIQR ARTNARLAGI GELITFEVKD VAQLTNPLPK
     EPYGTVLSNP PYGERLDSEP ALIALHSLLG RIMKNQFGGW NLSLFSASPD LLSCLQLRAD
     KQYKAKNGPL DCVQKNYHVA ESTPDSKPAM VAEDYANRLR KNLKKFEKWA RQEGIECYRL
     YDADLPEYNV AVDRYADWVV VQEYAPPKTI DAHKARQRLF DIIAATISVL GIAPNKLVLK
     TRERQKGKNQ YQKLGEKGEF LEVTEYNAHL WVNLTDYLDT GLFLDHRIAR RMLGQMSKGK
     DFLNLFSYTG SATVHAGLGG ARSTTTVDMS RTYLEWAERN LRLNGLTGRA HRLIQADCLA
     WLREANEQFD LIFIDPPTFS NSKRMEDAFD VQRDHLALMK DLKRLLRAGG TIMFSNNKRG
     FRMDLDGLAK LGLKAQEITQ KTLSQDFARN RQIHNCWLIT AA
//

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