(data stored in SCRATCH zone)

SWISSPROT: C8W2R8_DESAS

ID   C8W2R8_DESAS            Unreviewed;       305 AA.
AC   C8W2R8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607};
DE            EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Name=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   OrderedLocusNames=Dtox_0111 {ECO:0000313|EMBL:ACV61074.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61074.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61074.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518
CC       and A1519) in the loop of a conserved hairpin near the 3'-end of
CC       16S rRNA in the 30S particle. May play a critical role in
CC       biogenesis of 30S subunits. {ECO:0000256|HAMAP-Rule:MF_00607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-
CC         adenosyl-L-methionine = 4 H(+) + N(6)-
CC         dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA
CC         + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19609, Rhea:RHEA-
CC         COMP:10232, Rhea:RHEA-COMP:10233, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74493; EC=2.1.1.182; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00344807}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC       family. RsmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00540765}.
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DR   EMBL; CP001720; ACV61074.1; -; Genomic_DNA.
DR   RefSeq; WP_012813526.1; NC_013216.1.
DR   STRING; 485916.Dtox_0111; -.
DR   EnsemblBacteria; ACV61074; ACV61074; Dtox_0111.
DR   KEGG; dae:Dtox_0111; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
DR   OrthoDB; 2030110at2; -.
DR   BioCyc; DACE485916:G1GFV-117-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.100; -; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W2R8.
DR   SWISS-2DPAGE; C8W2R8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00423242};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314905};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00445489};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00423218};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314911,
KW   ECO:0000313|EMBL:ACV61074.1}.
FT   DOMAIN       35    212       rADc. {ECO:0000259|SMART:SM00650}.
FT   BINDING      28     28       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      30     30       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00607, ECO:0000256|PROSITE-ProRule:
FT                                PRU01026}.
FT   BINDING      55     55       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      76     76       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     101    101       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     127    127       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
SQ   SEQUENCE   305 AA;  34748 MW;  30DD5C75C040FF07 CRC64;
     MSELSSPSKV FNLFKEFNFH TNKKLGQNFL IDSNIISKII SAADLRSEDL VVEIGPGLGV
     LTQSIADEVS RVLSIEIDRK LQPILEVNLK EYSNTKVIFQ DALKTDFDRL VYAEAGGKSR
     SYKVIANLPY YITTPLLMHI LESKFNVELI VIMVQREVAE RMTAPPGKKD YGALSVAVQY
     YTEPEIICRV PKTVFIPAPE VDSTVIRLIK RKLPPVQLKS EKLFFNLVRT AFNQRRKTVL
     NAMQGSNWGL MKEEWKIILE KAGIDPMRRG ETFSLQDFAM LSNCVYETLK ELSTVYQEGE
     QIPLY
//

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