(data stored in SCRATCH zone)

SWISSPROT: C5B7P1_EDWI9

ID   C5B7P1_EDWI9            Unreviewed;       271 AA.
AC   C5B7P1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 63.
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=NT01EI_0696 {ECO:0000313|EMBL:ACR67918.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67918.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: 4 S-adenosyl-L-methionine +
CC       adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-
CC       homocysteine + N(6)-dimethyladenine(1518)/N(6)-
CC       dimethyladenine(1519) in 16S rRNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00607}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00633798}.
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:SAAS00633788}.
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DR   EMBL; CP001600; ACR67918.2; -; Genomic_DNA.
DR   RefSeq; WP_015870111.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0696; -.
DR   EnsemblBacteria; ACR67918; ACR67918; NT01EI_0696.
DR   GeneID; 7962030; -.
DR   KEGG; eic:NT01EI_0696; -.
DR   PATRIC; fig|634503.3.peg.627; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OrthoDB; POG091H02E3; -.
DR   Proteomes; UP000001485; 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; C5B7P1.
DR   SWISS-2DPAGE; C5B7P1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00633772};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633775,
KW   ECO:0000313|EMBL:ACR67918.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633771};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00644568};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633825};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633791,
KW   ECO:0000313|EMBL:ACR67918.2}.
FT   DOMAIN       25    198       rADc. {ECO:0000259|SMART:SM00650}.
FT   BINDING      18     18       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      20     20       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00607, ECO:0000256|PROSITE-ProRule:
FT                                PRU01026}.
FT   BINDING      45     45       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      66     66       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      91     91       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     113    113       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
SQ   SEQUENCE   271 AA;  30368 MW;  155255C7D25935F9 CRC64;
     MNSRVHQGHL ARKRFGQNFL TDQFVIDSIV SAINPLPGQA VVEIGPGLGA LTEPVADRMD
     KMTVVELDRD LAERLSTHPF ISRKLTIRQQ DAMTVDFSEM AREAGQPLRV FGNLPYNIST
     PLMFHLFSYA SAISDMHFML QKEVVNRLVA GPDSKTYGRL SVMAQYYCQV VPVLEVPPSA
     FRPAPKVDSA VVRLIPHREL PYPVSDVRVL SRITTEAFNQ RRKTIRNSLG HLFSADQLSA
     LGIDPARRAE TLSVADYCRL ANWLCEHPQA Q
//

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