(data stored in SCRATCH zone)

SWISSPROT: TRMK_BACSU

ID   TRMK_BACSU              Reviewed;         238 AA.
AC   P54471;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=tRNA (adenine(22)-N(1))-methyltransferase;
DE            EC=2.1.1.217;
DE   AltName: Full=TrMet(m1A22);
DE   AltName: Full=tRNA(m1A22)-methyltransferase;
DE            Short=tRNA(m1A22)MTase;
GN   Name=trmK; Synonyms=yqfN; OrderedLocusNames=BSU25180;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION OF START CODON.
RC   STRAIN=168;
RX   PubMed=18420655; DOI=10.1093/nar/gkn169;
RA   Roovers M., Kaminska K.H., Tkaczuk K.L., Gigot D., Droogmans L.,
RA   Bujnicki J.M.;
RT   "The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase
RT   (TrmK).";
RL   Nucleic Acids Res. 36:3252-3262(2008).
CC   -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC       N(1)-methyladenine at position 22 (m1A22) in tRNA.
CC       {ECO:0000269|PubMed:18420655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(22) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methyladenosine(22) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43144, Rhea:RHEA-COMP:10361, Rhea:RHEA-COMP:10362,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.217;
CC         Evidence={ECO:0000269|PubMed:18420655};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TrmK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB14448.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; D84432; BAA12491.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB14448.1; ALT_INIT; Genomic_DNA.
DR   PIR; H69953; H69953.
DR   RefSeq; NP_390397.1; NC_000964.3.
DR   RefSeq; WP_003246178.1; NC_000964.3.
DR   PDB; 6Q56; X-ray; 2.00 A; A/B/C/D=1-238.
DR   PDBsum; 6Q56; -.
DR   SMR; P54471; -.
DR   STRING; 224308.BSU25180; -.
DR   iPTMnet; P54471; -.
DR   jPOST; P54471; -.
DR   PaxDb; P54471; -.
DR   PRIDE; P54471; -.
DR   DNASU; 937898; -.
DR   EnsemblBacteria; CAB14448; CAB14448; BSU25180.
DR   GeneID; 937898; -.
DR   KEGG; bsu:BSU25180; -.
DR   PATRIC; fig|224308.43.peg.2625; -.
DR   eggNOG; COG2384; LUCA.
DR   HOGENOM; HOG000014372; -.
DR   InParanoid; P54471; -.
DR   KO; K06967; -.
DR   BioCyc; BSUB:BSU25180-MONOMER; -.
DR   BioCyc; MetaCyc:BSU25180-MONOMER; -.
DR   BRENDA; 2.1.1.217; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR006901; TrmK.
DR   Pfam; PF04816; TrmK; 1.
DR   PIRSF; PIRSF018637; TrmK; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54471.
DR   SWISS-2DPAGE; P54471.
KW   3D-structure; Cytoplasm; Methyltransferase; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..238
FT                   /note="tRNA (adenine(22)-N(1))-methyltransferase"
FT                   /id="PRO_0000049798"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   HELIX           8..14
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          21..26
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           32..39
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          42..52
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           53..65
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   TURN            69..71
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          72..78
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           79..82
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          89..96
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           98..107
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           109..111
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          116..124
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           127..135
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          139..148
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   STRAND          151..161
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           165..167
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           172..178
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           180..185
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           188..210
FT                   /evidence="ECO:0000244|PDB:6Q56"
FT   HELIX           215..234
FT                   /evidence="ECO:0000244|PDB:6Q56"
SQ   SEQUENCE   238 AA;  26162 MW;  F59DA3FB5091C0C9 CRC64;
     MNELKLSKRL QTVAEYIPNG AVMADIGSDH AYLPCYAVLN HKASGAIAGE ITDGPFLSAK
     RQVEKSGLNS HISVRQGDGL EVIKKGEADA ITIAGMGGAL IAHILEAGKD KLTGKERLIL
     QPNIHAVHIR EWLYKERYAL IDEVILEEDG KCYEVLVAEA GDRDAAYDGI SLSAGMLVGP
     FLAKEKNAVF LKKWTQELQH TQSIYEQISQ AADTEQNKQK LKELADRMEL LKEVIDHG
//

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