(data stored in ACNUC7421 zone)

SWISSPROT: A0KEW8_AERHH

ID   A0KEW8_AERHH            Unreviewed;       430 AA.
AC   A0KEW8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:ABK37178.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ABK37178.1};
GN   Name=sun {ECO:0000313|EMBL:ABK37178.1};
GN   OrderedLocusNames=AHA_0256 {ECO:0000313|EMBL:ABK37178.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37178.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37178.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|SAAS:SAAS01079038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219,
CC         Rhea:RHEA-COMP:10220, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         EC=2.1.1.176; Evidence={ECO:0000256|SAAS:SAAS01116325};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00029836}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023,
CC       ECO:0000256|SAAS:SAAS00546407}.
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DR   EMBL; CP000462; ABK37178.1; -; Genomic_DNA.
DR   RefSeq; WP_011704264.1; NC_008570.1.
DR   RefSeq; YP_854784.1; NC_008570.1.
DR   STRING; 380703.AHA_0256; -.
DR   EnsemblBacteria; ABK37178; ABK37178; AHA_0256.
DR   GeneID; 4486957; -.
DR   KEGG; aha:AHA_0256; -.
DR   PATRIC; fig|380703.7.peg.243; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   BioCyc; AHYD380703:G1G7B-257-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEW8.
DR   SWISS-2DPAGE; A0KEW8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221280, ECO:0000313|EMBL:ABK37178.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS01090267};
KW   rRNA processing {ECO:0000256|SAAS:SAAS00149471};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00500162};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221314, ECO:0000313|EMBL:ABK37178.1}.
FT   DOMAIN      161    430       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   REGION      251    257       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   ACT_SITE    373    373       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     275    275       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     301    301       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     320    320       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   430 AA;  47981 MW;  AEC3F905DC7AC162 CRC64;
     MKTRAQAALV IQQVLDQGQS LSAVLPAAQE KVAPRDRALL QELCYGTLRW LPRLDAAVGE
     MMDKPLKNKS RIFHYLILVG LYQLIYTRIP AHAAVAETVN AVKLLKGTSL RGLINGVLRN
     FQRSAEVILL RIDRVPSIRL GHPEWLTKRL RQAYPDEWEF IMEANNQRPP MWIRNNSQRQ
     SREQMLVRMA EAGINAMAGE EGEDCILLER PCDVTKLPGF EAGDCSVQDG AAQQAAALLD
     PQPGEWVLDA CAAPGGKTAH LLERQPALAG VVAVDADDNR LKRVQENLDR IGLTAKVIHG
     DASTPDLWWP EGQFDRILLD APCSATGVIR RHPDIKWLRR DQDIRELAEL QHRILGALWS
     KLKSGGTLLY ATCSVLPEEN RDQIRAFLAA TPDATLVPLH AQDTPECPGR QFLPGEAEMD
     GFYYAKLIKR
//

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