(data stored in SCRATCH zone)

SWISSPROT: C4KJF9_SULIK

ID   C4KJF9_SULIK            Unreviewed;       223 AA.
AC   C4KJF9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 35.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase Nep1 {ECO:0000256|HAMAP-Rule:MF_00554};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00554};
DE   AltName: Full=16S rRNA (pseudouridine-N1-)-methyltransferase Nep1 {ECO:0000256|HAMAP-Rule:MF_00554};
GN   Name=nep1 {ECO:0000256|HAMAP-Rule:MF_00554};
GN   OrderedLocusNames=M164_0043 {ECO:0000313|EMBL:ACR40679.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40679.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40679.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Methyltransferase involved in ribosomal biogenesis.
CC       Specifically catalyzes the N1-methylation of the pseudouridine
CC       corresponding to position 914 in M.jannaschii 16S rRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_00554}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a pseudouridine in
CC       16S rRNA = S-adenosyl-L-homocysteine + a N(1)-methylpseudouridine
CC       in 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_00554}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00554}.
CC   -!- SIMILARITY: Belongs to the NEP1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00554}.
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DR   EMBL; CP001402; ACR40679.1; -; Genomic_DNA.
DR   RefSeq; WP_012710222.1; NC_012726.1.
DR   EnsemblBacteria; ACR40679; ACR40679; M164_0043.
DR   GeneID; 8759882; -.
DR   KEGG; sid:M164_0043; -.
DR   HOGENOM; HOG000109939; -.
DR   KO; K14568; -.
DR   OMA; TRLPRNY; -.
DR   OrthoDB; POG093Z0AR9; -.
DR   BioCyc; SISL426118:GI01-43-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00554; NEP1; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR   InterPro; IPR023503; Ribosome_NEP1_arc.
DR   PANTHER; PTHR12636; PTHR12636; 1.
DR   Pfam; PF03587; EMG1; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJF9.
DR   SWISS-2DPAGE; C4KJF9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00554};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00554};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00554};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00554};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00554};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00554};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00554}.
FT   REGION      199    204       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00554}.
FT   BINDING     177    177       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00554}.
FT   BINDING     182    182       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00554}.
FT   SITE         66     66       Interaction with substrate rRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00554}.
FT   SITE         68     68       Stabilizes Arg-xx. {ECO:0000256|HAMAP-
FT                                Rule:MF_00554}.
FT   SITE        104    104       Interaction with substrate rRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00554}.
FT   SITE        107    107       Interaction with substrate rRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00554}.
FT   SITE        111    111       Interaction with substrate rRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00554}.
SQ   SEQUENCE   223 AA;  25602 MW;  410883C6E3D8FE8E CRC64;
     MLKYSMHLNI VLLEASLELV PKEIVNHPAV IKNAKRRNKK PEETLLDISL HYHAMKSLEN
     SHKRGRPDIL HQALLVILND PVIKGDLFIH TIQSKIIKVN PNMRPPKNYL RFMGLMEQLL
     KYGRIPINGD ESLMEVTNLT LEEIAARYNL ILLSEKGEKI NPEELCKLDE KWILGIGTFP
     HGDFSEKILS LAKKIYSISE FQLETQQVLC RIFSACNSIL GWP
//

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