(data stored in SCRATCH zone)

SWISSPROT: Q500T1_PSEU2

ID   Q500T1_PSEU2            Unreviewed;       448 AA.
AC   Q500T1;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   SubName: Full=16S rRNA m(5)C-967 methyltransferase {ECO:0000313|EMBL:AAY35091.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:AAY35091.1};
GN   OrderedLocusNames=Psyr_0017 {ECO:0000313|EMBL:AAY35091.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35091.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35091.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35091.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35091.1; -; Genomic_DNA.
DR   RefSeq; WP_011266131.1; NC_007005.1.
DR   RefSeq; YP_233129.1; NC_007005.1.
DR   STRING; 205918.Psyr_0017; -.
DR   EnsemblBacteria; AAY35091; AAY35091; Psyr_0017.
DR   GeneID; 3365492; -.
DR   KEGG; psb:Psyr_0017; -.
DR   PATRIC; fig|205918.7.peg.17; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   BioCyc; PSYR205918:G1G4J-17-MONOMER; -.
DR   Proteomes; UP000000426; 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; Q500T1.
DR   SWISS-2DPAGE; Q500T1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00221280, ECO:0000313|EMBL:AAY35091.1};
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:AAY35091.1}.
FT   DOMAIN      161    436       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   448 AA;  48390 MW;  EB4DE6EADD8630DC CRC64;
     MNPRLAAAKA LAAVLSGKAS LNSSLPTQLD KVEVRDRGLT QDLAFGTARW QPRLSALAAK
     LLQKPFKAAD ADVEALLLVG LYQLFYSRIP AHAAIGETVG CADKLKKPWA KGLLNAVLRN
     AQRDGEALLI ELEHDPVVRT AHPRWLQKAL KAAWPEQWEA ICAANNAHPP MILRVNRRHH
     RRDQYLELLD TAGLQASACT FSQDGIVLAE PCDVRSLPGF AEGWISVQDE AAQLAADLLE
     LAPGQRVLDA CCAPGGKTCH LLEVQPQLDG VVAVDLEAKR LVRVRENLDR LGLDAELIAA
     DARETAQWWD GKPFQRILLD APCSATGVIR RHPDIKLTRQ ADDIAALAAL QGELLDALWP
     TLQVGGMLVY ATCSTLPTEN TDVIEAFLAR TSGARELDIA GQAGQPPAGI KQAHGRQLLA
     QQGGHDGFYY AKLIKIADQD RGGAGVSA
//

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