SYMC_SCHPO
ID SYMC_SCHPO Reviewed; 782 AA.
AC Q9UUF2; O13634;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=rar1; Synonyms=mes1, mrs1; ORFNames=pi042, SPBC17A3.04c;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB004537; BAA21422.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAB51763.1; -; Genomic_DNA.
DR PIR; T39696; T39696.
DR RefSeq; NP_595586.1; NM_001021482.2.
DR AlphaFoldDB; Q9UUF2; -.
DR SMR; Q9UUF2; -.
DR BioGRID; 276590; 5.
DR STRING; 4896.SPBC17A3.04c.1; -.
DR iPTMnet; Q9UUF2; -.
DR MaxQB; Q9UUF2; -.
DR PaxDb; Q9UUF2; -.
DR PRIDE; Q9UUF2; -.
DR EnsemblFungi; SPBC17A3.04c.1; SPBC17A3.04c.1:pep; SPBC17A3.04c.
DR GeneID; 2540052; -.
DR KEGG; spo:SPBC17A3.04c; -.
DR PomBase; SPBC17A3.04c; rar1.
DR VEuPathDB; FungiDB:SPBC17A3.04c; -.
DR eggNOG; KOG1247; Eukaryota.
DR HOGENOM; CLU_009710_4_1_1; -.
DR InParanoid; Q9UUF2; -.
DR OMA; YMRMAGH; -.
DR PhylomeDB; Q9UUF2; -.
DR PRO; PR:Q9UUF2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IPI:PomBase.
DR GO; GO:0005844; C:polysome; EXP:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..782
FT /note="Probable methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000139268"
FT MOTIF 231..241
FT /note="'HIGH' region"
FT MOTIF 551..555
FT /note="'KMSKS' region"
SQ SEQUENCE 782 AA; 88881 MW; DAB49CB4758748C2 CRC64;
MATYKVQIPA SFKTSYSFAE SLKVSIAISA FSVKVPCEGA ANCNSVRLVN SKEPEKYVSD
ANAIVSFLYW KQEEDLFNSF ISSKLSILDW EALQFTPKAY TAKTKEDFAY LLSQLETIFK
ENEILNEFTP VEVALASDIY FCVLNGAPVR EYPLLSAWYL KIEKQKPFVQ ALKLTFEKTL
GQPAVTSTEK IPVSETTRNV NSQHLMRERV PGEKILPKSN ERNILITSAL PYVNNVPHLG
NIVGSTLSAD VFARYHRARN HNTLYICGTD EYGTATETKA LEEGVSPKEL CDKYHALHKE
VYDWFEIDFD HFGRTTTPKQ TGIAQHIFTK LYNNDYMAID TMTQLYCEVH QGYLADRYVE
GTCPKCGYDD ARGDQCDGCG GLLNAFELID PKCKLDRATP VKRETKHVFL SLDKLQPAVE
SWAMQSAVEG KWSNNGRSIT ESWLKEGLRP RCITRDLKWG TPVPLEEFKG KVLYVWFDAT
IGYISITANY TDEWEKWWRN PEQVKLYQFM GKDNVPFHTV IFPSSLLGTG EKWTMLHHIN
TTDYLNYETG KFSKSRGVGV FGNTAQDIGL SPSVWRYYLL SSRPETSDTM FTWKEFITRH
NSELLANLGN FVNRTLKFTT AKYNGLVPHY LTDPSVGAGK LKADFVKDVN ALLAKYNAAL
EASKLREGLR LAMEISARGN QYLQDNRIDN KCYLYERQKC ADAIGYALNL IYLLAAIFYP
YMPSTSTSIY KQLNAPAAAI PDTWELCLLP GHRIGEPEYL FTRIDESMEE EWRSKYGGNG
SN
