ARC1_SCHPO
ID ARC1_SCHPO Reviewed; 450 AA.
AC Q9P6K7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=tRNA-aminoacylation cofactor arc1;
GN ORFNames=SPAC30C2.04;
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: Binds to tRNA and functions as a cofactor for the methionyl-
CC tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a
CC complex with MetRS and GluRS and increases their affinity for cognate
CC tRNAs due to the presence of a tRNA binding domain in its middle and C-
CC terminal part (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a yeast aminoacyl-tRNA synthase (aaRS) complex
CC formed by methionyl-tRNA synthase, glutamyl-tRNA synthase and the tRNA
CC aminoacylation cofactor arc1 in a stoichiometric complex. Interacts
CC with rar1/mes1 and gus1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the tRNA-aminoacylation cofactor ARC1 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB90791.1; -; Genomic_DNA.
DR RefSeq; NP_594656.1; NM_001020085.2.
DR AlphaFoldDB; Q9P6K7; -.
DR SMR; Q9P6K7; -.
DR BioGRID; 279520; 58.
DR STRING; 4896.SPAC30C2.04.1; -.
DR iPTMnet; Q9P6K7; -.
DR MaxQB; Q9P6K7; -.
DR PaxDb; Q9P6K7; -.
DR PRIDE; Q9P6K7; -.
DR EnsemblFungi; SPAC30C2.04.1; SPAC30C2.04.1:pep; SPAC30C2.04.
DR GeneID; 2543087; -.
DR KEGG; spo:SPAC30C2.04; -.
DR PomBase; SPAC30C2.04; -.
DR VEuPathDB; FungiDB:SPAC30C2.04; -.
DR eggNOG; KOG2241; Eukaryota.
DR HOGENOM; CLU_009710_6_6_1; -.
DR InParanoid; Q9P6K7; -.
DR OMA; PAPWMID; -.
DR PhylomeDB; Q9P6K7; -.
DR PRO; PR:Q9P6K7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:PomBase.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IPI:PomBase.
DR GO; GO:0005844; C:polysome; EXP:PomBase.
DR GO; GO:0000049; F:tRNA binding; ISO:PomBase.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:PomBase.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; ISO:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..450
FT /note="tRNA-aminoacylation cofactor arc1"
FT /id="PRO_0000317099"
FT DOMAIN 278..382
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 208..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 50606 MW; 21994251A1C0F9DE CRC64;
MSFLWAKEFC VLKYPYKLFI THKFSYLLRF ETVTLNNIRS PQFYAKLTFS HHQPTVSGTM
STELKFISKY LQISIPETKE GPVSSLFKAV SEQKPELLGN TDFEKAQILE WTTKAFSPIE
TQSIVEQLDE FLKSSTFIAQ DSGISVADLA VYARIHSYIC GLSAKEGYKL NNVCRWFDFI
QHQESVMEAA NSMSMKLANI DLNAPKIQRP SVIKKDKKEK KEGKPSQEAS VKSVEKAPKG
LEGAKKEKQN KKEKKDKKDK KDKKEKAPKE PPKAATPVPS MIDFRIGFIE KAVKHPNADS
LYVSTIHCGD AEGPRTVCSG LVKYIPLEQM QQRKVIVVAN LKPVNMRSVK SQAMVFCASS
PDKSVVEFVL PPENAEIGDR LTFEGFDTEE PEAQLNPKRK IWEAIQPGFT SGEDLICGYK
DESGLHRLFV KGKKDLGFCK AQTVVNGTLS
