MTQ1_SCHPO
ID MTQ1_SCHPO Reviewed; 309 AA.
AC O14028;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable MRF1 mitochondrial N(5)-glutamine methyltransferase mtq1;
DE EC=2.1.1.297 {ECO:0000250|UniProtKB:P53944};
GN Name=mtq1; ORFNames=SPAC29B12.05c;
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).
CC -!- FUNCTION: Methylates MRF1 on 'Gln-270' using S-adenosyl L-methionine as
CC methyl donor. {ECO:0000250|UniProtKB:P53944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000250|UniProtKB:P53944};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53944}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16250.1; -; Genomic_DNA.
DR PIR; T38493; T38493.
DR RefSeq; NP_594983.1; NM_001020414.2.
DR AlphaFoldDB; O14028; -.
DR SMR; O14028; -.
DR BioGRID; 279150; 1.
DR STRING; 4896.SPAC29B12.05c.1; -.
DR PaxDb; O14028; -.
DR EnsemblFungi; SPAC29B12.05c.1; SPAC29B12.05c.1:pep; SPAC29B12.05c.
DR GeneID; 2542697; -.
DR KEGG; spo:SPAC29B12.05c; -.
DR PomBase; SPAC29B12.05c; mtq1.
DR VEuPathDB; FungiDB:SPAC29B12.05c; -.
DR eggNOG; KOG2904; Eukaryota.
DR HOGENOM; CLU_018398_0_2_1; -.
DR InParanoid; O14028; -.
DR OMA; SYEPQNA; -.
DR PhylomeDB; O14028; -.
DR PRO; PR:O14028; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; ISS:PomBase.
DR GO; GO:0070126; P:mitochondrial translational termination; IC:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..309
FT /note="Probable MRF1 mitochondrial N(5)-glutamine
FT methyltransferase mtq1"
FT /id="PRO_0000353824"
FT BINDING 124..128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 200..203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 35771 MW; 1E70E15E1A395040 CRC64;
MRLPRITKFA LYRENPCLLP LYHATRDPSL AKREWTWICK ELKLLYPEIS KHGLRKKIVN
ACQLRARNYP LQYILKSQPF GNIKIDCQQG VLIPRWETEE WVERVVDKLN RLERLKPLKI
LDLCTGSGCI SSFVLANLRV PHTIEAVDVS KKALKLAVKN CDRAIAHGTV GKINFHQIDV
LNEHERVESL LQTSHVLLCN PPYISDDDFA AQTDISVRKY EPKLALLAKN GGNEFYYKFS
QYIKRMLQRN AKDFVPLSLI VFEIGSTHQA KIVKSLFDDT NWQANIEQDG AHQDRVVIIT
RKDRRLIDI
