(data stored in SCRATCH zone)

SWISSPROT: A8FP73_SHESH

ID   A8FP73_SHESH            Unreviewed;       426 AA.
AC   A8FP73;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   SubName: Full=Sun protein {ECO:0000313|EMBL:ABV34646.1};
GN   OrderedLocusNames=Ssed_0033 {ECO:0000313|EMBL:ABV34646.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34646.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34646.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34646.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34646.1; -; Genomic_DNA.
DR   RefSeq; WP_012004172.1; NC_009831.1.
DR   STRING; 425104.Ssed_0033; -.
DR   EnsemblBacteria; ABV34646; ABV34646; Ssed_0033.
DR   KEGG; sse:Ssed_0033; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   OrthoDB; 1064993at2; -.
DR   BioCyc; SSED425104:G1G9Y-34-MONOMER; -.
DR   Proteomes; UP000002015; 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; A8FP73.
DR   SWISS-2DPAGE; A8FP73.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221280};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
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}.
FT   DOMAIN      159    426       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   REGION      248    254       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   COILED      270    290       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    369    369       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     271    271       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     297    297       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     316    316       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   426 AA;  47625 MW;  BA54F12395F79567 CRC64;
     MNLRALAAKV VFQVLEKGIS LSVALPDQQR HLESGKDKAL MAELCYGVMR HLPQLDKLVS
     DCMSKPLKGK QRILHQLLLV GCYQLYFTRI PSHAAISETA EACRQLKFEG LVKVVNGVLR
     NIQRQEKPLP TDNETLALNT PAWIIKRLKA AYPESWKEIV EQSHQRPPMW LRSNKLSQTR
     DEYLASLAEV EIQASAGKSS DAILLESPKD VLQLPGFEEG TASVQDGAAQ WAATLLAPID
     GELVLDACAA PGGKTCHLLE QAPNIELVAV DFDANRLERV QQNLDRLSLN AKLIHGDAAD
     IDSWWQGDKF DRILLDAPCS ATGVIRRHPD IKWLRKQADI EELASLQSKI LDHCWQWLKP
     GGTLLYATCS ILPQENEQQI RAFLERANDA TLVPIDEQNH PDDIGWQITP GLENMDGFYY
     ARLVKG
//

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