TRM10_SCHPO
ID TRM10_SCHPO Reviewed; 304 AA.
AC O14214;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000303|PubMed:24081582};
DE EC=2.1.1.221 {ECO:0000269|PubMed:24081582};
DE AltName: Full=tRNA methyltransferase 10 {ECO:0000303|PubMed:24081582};
DE AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000303|PubMed:24081582};
DE Short=tRNA(m1G9)MTase {ECO:0000303|PubMed:24081582};
GN Name=trm10 {ECO:0000303|PubMed:24081582}; ORFNames=SPAC6B12.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF LYS-110; GLN-118;
RP ARG-121; ARG-127; ARG-147; LYS-153; VAL-206; ASP-207; LYS-208; ASN-209 AND
RP THR-244.
RX PubMed=24081582; DOI=10.1093/nar/gkt869;
RA Shao Z., Yan W., Peng J., Zuo X., Zou Y., Li F., Gong D., Ma R., Wu J.,
RA Shi Y., Zhang Z., Teng M., Li X., Gong Q.;
RT "Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the
RT catalytic mechanism and recognition of tRNA substrate.";
RL Nucleic Acids Res. 42:509-525(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-
CC methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC position 9 (m1G9) in cytoplasmic tRNA. {ECO:0000269|PubMed:24081582}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000269|PubMed:24081582};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for tRNA(Gly) {ECO:0000269|PubMed:24081582};
CC Note=kcat is 0.16 min(-1) for tRNA(Gly) (m1G9)-methylation.
CC {ECO:0000269|PubMed:24081582};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24081582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus
CC {ECO:0000250|UniProtKB:Q12400}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; CU329670; CAB11070.1; -; Genomic_DNA.
DR PIR; T39016; T39016.
DR RefSeq; NP_593764.1; NM_001019194.2.
DR PDB; 4JWF; X-ray; 2.40 A; A/B=74-281.
DR PDB; 4JWG; X-ray; 2.50 A; A=74-281.
DR PDB; 4JWH; X-ray; 2.04 A; A/B=1-304.
DR PDBsum; 4JWF; -.
DR PDBsum; 4JWG; -.
DR PDBsum; 4JWH; -.
DR AlphaFoldDB; O14214; -.
DR SMR; O14214; -.
DR BioGRID; 279743; 129.
DR STRING; 4896.SPAC6B12.09.1; -.
DR iPTMnet; O14214; -.
DR MaxQB; O14214; -.
DR PaxDb; O14214; -.
DR PRIDE; O14214; -.
DR EnsemblFungi; SPAC6B12.09.1; SPAC6B12.09.1:pep; SPAC6B12.09.
DR GeneID; 2543319; -.
DR KEGG; spo:SPAC6B12.09; -.
DR PomBase; SPAC6B12.09; trm10.
DR VEuPathDB; FungiDB:SPAC6B12.09; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_7_0_1; -.
DR InParanoid; O14214; -.
DR OMA; FKKNDGW; -.
DR PhylomeDB; O14214; -.
DR BRENDA; 2.1.1.221; 5613.
DR PRO; PR:O14214; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IDA:PomBase.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IDA:PomBase.
DR DisProt; DP00798; -.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR016653; TRM10/TRM10A.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF016323; tRNA_m1G_mtfrase_met; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..304
FT /note="tRNA (guanine(9)-N1)-methyltransferase"
FT /id="PRO_0000060518"
FT DOMAIN 81..276
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 207..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT BINDING 241..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24081582"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 110
FT /note="K->E: Completely abolishes interaction with tRNA;
FT when associated with E-121 and E-127."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 118
FT /note="Q->A: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 121
FT /note="R->E: Completely abolishes interaction with tRNA;
FT when associated with E-110 and E-127."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 127
FT /note="R->E: Completely abolishes interaction with tRNA;
FT when associated with E-110 and E-121."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 147
FT /note="R->E: Completely abolishes interaction with tRNA;
FT when associated with E-153."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 153
FT /note="K->E: Completely abolishes interaction with tRNA;
FT when associated with E-147."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 206
FT /note="V->A: Reduces catalytic activity to 19%."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 207
FT /note="D->N: Completely abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 208
FT /note="K->A: Reduces catalytic activity to 72%."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 209
FT /note="N->A: Has weaker affinity for S-adenosyl-L-
FT methionine and reduces catalytic activity to 10%."
FT /evidence="ECO:0000269|PubMed:24081582"
FT MUTAGEN 244
FT /note="T->A: Reduces catalytic activity to 35%."
FT /evidence="ECO:0000269|PubMed:24081582"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 109..128
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4JWG"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4JWH"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:4JWH"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4JWF"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:4JWH"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:4JWH"
SQ SEQUENCE 304 AA; 35470 MW; C41B7EE19741BFC8 CRC64;
MENKDALDIG KDDTNTSEAD VSKNETQEQP VLSKSALKRL KRQQEWDAGR EKRAEMRREK
KRLRKEERKR KIEAGEVVKS QKKRIRLGKV VPSSIRIVLD CAFDDLMNDK EINSLCQQVT
RCHSANRTAL HPVELFATNF GGRLKTRQDF VLKGQQNNWK RYNPTTKSYL EEFESQKEKL
VYLSADSDNT ITELDEDKIY IIGAIVDKNR YKNLCQNKAS EQGIKTAKLP IDEYIKITDR
KILTVNQVFE ILSLWLEYRD WEKAFMEVIP KRKGILLKSD ESFDVSEDTR SQSNQSDSEL
EKEN
