SYPM_YEAST
ID SYPM_YEAST Reviewed; 576 AA.
AC P39965; D3DLZ3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Probable proline--tRNA ligase, mitochondrial;
DE EC=6.1.1.15;
DE AltName: Full=Altered inheritance rate of mitochondria protein 10;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=AIM10; OrderedLocusNames=YER087W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 477 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; U18839; AAB64642.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07747.1; -; Genomic_DNA.
DR PIR; S50590; S50590.
DR RefSeq; NP_011010.1; NM_001178978.1.
DR AlphaFoldDB; P39965; -.
DR SMR; P39965; -.
DR BioGRID; 36831; 81.
DR DIP; DIP-4922N; -.
DR IntAct; P39965; 2.
DR MINT; P39965; -.
DR STRING; 4932.YER087W; -.
DR iPTMnet; P39965; -.
DR MaxQB; P39965; -.
DR PaxDb; P39965; -.
DR PRIDE; P39965; -.
DR EnsemblFungi; YER087W_mRNA; YER087W; YER087W.
DR GeneID; 856820; -.
DR KEGG; sce:YER087W; -.
DR SGD; S000000889; AIM10.
DR VEuPathDB; FungiDB:YER087W; -.
DR eggNOG; KOG2324; Eukaryota.
DR GeneTree; ENSGT00390000010922; -.
DR HOGENOM; CLU_016739_0_0_1; -.
DR InParanoid; P39965; -.
DR OMA; NCDYAAN; -.
DR BioCyc; YEAST:G3O-30256-MON; -.
DR SABIO-RK; P39965; -.
DR PRO; PR:P39965; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39965; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; ISS:SGD.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 2.
DR TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..576
FT /note="Probable proline--tRNA ligase, mitochondrial"
FT /id="PRO_0000139354"
SQ SEQUENCE 576 AA; 65880 MW; D8C5BD76B47CCAF3 CRC64;
MLKYRTLSRS CHIFHPKSLS NNTLKSETTQ ELLQTVGFVR RSQVGLFQWL PLGLRSLNKV
SNAIRNRMDS DGGAIEVSLS AISSKALWQA TDRWNNSELF KLKDSKGKQY CLTATCEEDI
TDLMKNYIAS YKDMPITIYQ MTRKYRDEIR PRGGILRGRE FLMKDAYSFA SNEEDAFASF
QKLDDTYNKI FKDLKIPFVS AWADSGDIGG EFSKEFHLIH ESGEDTLMSC KHCGDISTLD
MSQSYPEKDG QYSGDVDCKY ALTKDHSTLI CFYYPKDRQL NWNLALNAMD KDIDLTLRNK
PNDHVLQVYE KDNEDIMFSK ILRVMDCRLN SKSNFPDFPL KKYLKNNFGQ ISDVSIVDAQ
ENEICGKCEE GRLEPLKSIE VGHIFLLGNK YSKPLNVKFV DKENKNETFV HMGCYGIGVS
RLVGAIAELG RDSNGFRWPA IMAPYKVSIC TGPNNPENSQ RLQDVKSELL NDPTMQNLQN
DILDQFNEKL GIGARIKLSH AMGIPLCVIV GSKSWPNVEI EVRGIRWGEK DLWRKQFEKR
CSELQWKCTK NEHGIEKHTV PIQHLAEVIG VLLKDM
