(data stored in ACNUC7421 zone)

SWISSPROT: A0LEK0_SYNFM

ID   A0LEK0_SYNFM            Unreviewed;       449 AA.
AC   A0LEK0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   SubName: Full=Sun protein {ECO:0000313|EMBL:ABK15852.1};
GN   OrderedLocusNames=Sfum_0150 {ECO:0000313|EMBL:ABK15852.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15852.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15852.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP000478; ABK15852.1; -; Genomic_DNA.
DR   RefSeq; WP_011697025.1; NC_008554.1.
DR   STRING; 335543.Sfum_0150; -.
DR   EnsemblBacteria; ABK15852; ABK15852; Sfum_0150.
DR   KEGG; sfu:Sfum_0150; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   OrthoDB; 1064993at2; -.
DR   BioCyc; SFUM335543:G1G7I-154-MONOMER; -.
DR   Proteomes; UP000001784; 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; A0LEK0.
DR   SWISS-2DPAGE; A0LEK0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221280};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
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      172    448       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    385    385       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     287    287       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     314    314       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     332    332       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   449 AA;  50949 MW;  BA453F228BEF9C8C CRC64;
     MINARVLAFQ ILLHMDRDAS HPDRLIRGML GRHERLEERD RALLTELVYG VLRWQGRLDW
     HIDQLSRTRP EKIDPAVRIL LRLALYQILM LDRIPDHAAV NEAVNMAKTT QPAYLVKFVN
     GVLREALRRR SRWIWPEAGE EPGKYIAVTT AHPIWYVERL LHEFGFEETL DICNANNTVA
     PMTLRVNALK TSIDTILQWC AEHGIDAEPS GVVPTAVRLS GLRRDLAETS IYRDGLVQVQ
     DEASQIVSTL VAPRAGERVL DLCAGFGGKS THLGILMGDR GEVVAVDNSA WKLEELRKNA
     RRQGLRIIKP RTADLFEFSP GTEDLFDRVL LDAPCSGFGT LRRNPDIKWR RHLKDPRRFG
     RIQKEMLDHA ARFVKPGGAL VYSACTLFQE ENDAVAEHFA ASHPDWQIEP VGPDLPDACR
     GMASGPFFRT WPHRHQVDGF FAARLKRPA
//

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