(data stored in SCRATCH zone)

SWISSPROT: C1ASQ4_RHOOB

ID   C1ASQ4_RHOOB            Unreviewed;       284 AA.
AC   C1ASQ4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 50.
DE   RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase TrmI {ECO:0000256|PIRNR:PIRNR017269};
DE            EC=2.1.1.220 {ECO:0000256|PIRNR:PIRNR017269};
GN   OrderedLocusNames=ROP_05890 {ECO:0000313|EMBL:BAH48836.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48836.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48836.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48836.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent
CC       formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
CC       {ECO:0000256|PIRNR:PIRNR017269}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(58) in tRNA
CC       = S-adenosyl-L-homocysteine + N(1)-methyladenine(58) in tRNA.
CC       {ECO:0000256|PIRNR:PIRNR017269}.
CC   -!- SUBUNIT: Homotetramer composed of a dimer of dimers.
CC       {ECO:0000256|PIRNR:PIRNR017269}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TRM61 family.
CC       {ECO:0000256|PIRNR:PIRNR017269}.
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DR   EMBL; AP011115; BAH48836.1; -; Genomic_DNA.
DR   RefSeq; WP_012687841.1; NC_012522.1.
DR   ProteinModelPortal; C1ASQ4; -.
DR   STRING; 632772.ROP_05890; -.
DR   EnsemblBacteria; BAH48836; BAH48836; ROP_05890.
DR   KEGG; rop:ROP_05890; -.
DR   PATRIC; fig|632772.20.peg.647; -.
DR   eggNOG; ENOG41066UU; Bacteria.
DR   eggNOG; COG2519; LUCA.
DR   HOGENOM; HOG000245274; -.
DR   KO; K07442; -.
DR   OMA; VVYPKDA; -.
DR   OrthoDB; POG091H0ATC; -.
DR   BioCyc; ROPA632772:GH0Q-588-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR   PANTHER; PTHR12133; PTHR12133; 1.
DR   Pfam; PF08704; GCD14; 1.
DR   PIRSF; PIRSF017269; GCD14; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51620; SAM_TRM61; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASQ4.
DR   SWISS-2DPAGE; C1ASQ4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR017269,
KW   ECO:0000313|EMBL:BAH48836.1};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR017269,
KW   ECO:0000256|PIRSR:PIRSR017269-1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR017269,
KW   ECO:0000313|EMBL:BAH48836.1};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR017269}.
FT   REGION      115    118       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR017269-1}.
FT   BINDING     136    136       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR017269-1}.
FT   BINDING     141    141       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR017269-1}.
FT   BINDING     166    166       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR017269-1}.
FT   BINDING     185    185       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR017269-1}.
SQ   SEQUENCE   284 AA;  30869 MW;  7A9367E52E8F759E CRC64;
     MVGRETRPSG PFRVGDRVQL TDGKGRHYTV NLEAGKEFHT HRGGILHDDL IGTDEGSVVK
     STNGTPYLAL RPLLTDYVLS MPRGAQVIYP KDAAQIVHEG DVFPGARVLE AGAGSGALTC
     SLLRAVGPEG RVISYEVRDD HAEHAVRNVE TFFGERPENW DLTIADVAEF DAEAAGGPVD
     RVVLDMLAPW DALPAVSKAL VPGGVLVVYV ATVTQLSKVV EAMREQECWT EPRSWESIVR
     GWHVVGLAVR PEHRMQGHTA FLVSARRLAE GTVTPKPQRR SGKG
//

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