MSS1_SCHPO
ID MSS1_SCHPO Reviewed; 496 AA.
AC Q9UTE7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=tRNA modification GTPase mss1, mitochondrial;
DE Flags: Precursor;
GN Name=mss1; ORFNames=SPAC222.05c;
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: GTPase involved in the 5-carboxymethylaminomethyl
CC modification (mnm(5)s(2)U34) of the wobble uridine base in
CC mitochondrial tRNAs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB60697.1; -; Genomic_DNA.
DR PIR; T50146; T50146.
DR RefSeq; NP_593144.1; NM_001018541.2.
DR AlphaFoldDB; Q9UTE7; -.
DR SMR; Q9UTE7; -.
DR BioGRID; 278438; 17.
DR STRING; 4896.SPAC222.05c.1; -.
DR SwissPalm; Q9UTE7; -.
DR MaxQB; Q9UTE7; -.
DR PaxDb; Q9UTE7; -.
DR EnsemblFungi; SPAC222.05c.1; SPAC222.05c.1:pep; SPAC222.05c.
DR GeneID; 2541951; -.
DR KEGG; spo:SPAC222.05c; -.
DR PomBase; SPAC222.05c; mss1.
DR VEuPathDB; FungiDB:SPAC222.05c; -.
DR eggNOG; KOG1191; Eukaryota.
DR HOGENOM; CLU_019624_3_1_1; -.
DR InParanoid; Q9UTE7; -.
DR OMA; CEIQCHG; -.
DR PhylomeDB; Q9UTE7; -.
DR PRO; PR:Q9UTE7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISS:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; NAS:PomBase.
DR GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; ISO:PomBase.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..496
FT /note="tRNA modification GTPase mss1, mitochondrial"
FT /id="PRO_0000035780"
FT DOMAIN 239..416
FT /note="TrmE-type G"
FT BINDING 246..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 293..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 363..366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 55316 MW; 092F7E1E1CDD80D2 CRC64;
MRILNRVFLN TFQACFRRFV HQIPTIYALS TPPGTSAVAI VRISGPNACK VAKTLAGSVP
KPRIASLRTI KHPVRSEVID KALMLYFKKP SSFTGEDVVE LQLHGGTAVV DVTLEAIKQS
GIPNIRYAKP GEFSERAFYN GRADLTQLEG LIDVINAQTA EQLYSANKEA HGSIYDICFR
WRKKLIEYRA FLEASIDFSE EHELDDIETI KLFEELNEMK DEIDAHIEGG KCKEVLRKGI
NVAILGPSNA GKSSLINLLA NRRISIVSPQ SGTTRDAIEV LVDINGFPVL LSDTAGLRKG
EDVQEIEKIG IEIAKARAEE SQLTLFVFPI NYHSFSESLK QSEILETIKD CLRQRKPIHF
LINKVDCVSD YTTMFKPIKA YLQKNFLIPE NRIHAVSCKT KEGLIDFLQA LSSTFECMVN
PLTNNKIQAN LGWNERQRQC LSSCSSHLSL ALQKSSDIVV AAEEVKLATE DIGRVTGAVD
MENVFSVIFS KFCVGK
