(data stored in ACNUC29543 zone)

SWISSPROT: A5GRG8_SYNR3

ID   A5GRG8_SYNR3            Unreviewed;       454 AA.
AC   A5GRG8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:CAK27477.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:CAK27477.1};
GN   Name=rsmB {ECO:0000313|EMBL:CAK27477.1};
GN   OrderedLocusNames=SynRCC307_0574 {ECO:0000313|EMBL:CAK27477.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27477.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27477.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK27477.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0574; -.
DR   EnsemblBacteria; CAK27477; CAK27477; SynRCC307_0574.
DR   KEGG; syr:SynRCC307_0574; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   BioCyc; SSP316278:G1GJL-560-MONOMER; -.
DR   Proteomes; UP000001115; 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; A5GRG8.
DR   SWISS-2DPAGE; A5GRG8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221280, ECO:0000313|EMBL:CAK27477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
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:CAK27477.1}.
FT   DOMAIN      190    454       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   REGION      283    289       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   ACT_SITE    405    405       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     307    307       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     334    334       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     352    352       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   454 AA;  49301 MW;  F8C481F0B6F92F09 CRC64;
     MSKGRCPCGA ICGHRSCPFV LSPDSAVGLP PRLVAWRVLE AVGDGAYADL ALERELKRSK
     LSPRDRGLAT ELAYGAIRQR RRLDGWLDLL GKVPAAKQPP RLRWLLHVGL QQILLMDRVP
     ASAAVSTAVE LAKRERLQRL APVVNGVLRA AVRAVEAGES LPVPSDPQKR LALEHSLPDW
     LVAELWGQIG PERTEALAAA SNRIPPLDLR CNRLRSSREA LLENLPAVAL AELPDGLTLT
     SRPGPLPQLA GFSEGQWCVQ DRAAQRIAPL LDPKPGQRVL DACAAPGGKT THIAELMGDQ
     GEVVAVDVAP RRLQQVSANA ERLGLSCIRT EAADATDLTD WEAESFDRVL LDVPCSGLGT
     LARHADARWN LKPDGIEELV GLQHQLLEQG ARLLKPDGRL VYATCTVHPA ENTGVVEAFV
     EENPDWQFSE PPMQLWPDPQ GGDGFFAAVL SLRR
//

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