SYFM_YEAST
ID SYFM_YEAST Reviewed; 469 AA.
AC P08425; D6W455; Q12410;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase;
DE Short=PheRS;
DE Flags: Precursor;
GN Name=MSF1; OrderedLocusNames=YPR047W; ORFNames=YP9499.05;
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 [GENOMIC DNA].
RX PubMed=3029120; DOI=10.1016/s0021-9258(18)61410-3;
RA Koerner T.J., Myers A.M., Lee S., Tzagoloff A.;
RT "Isolation and characterization of the yeast gene coding for the alpha
RT subunit of mitochondrial phenylalanyl-tRNA synthetase.";
RL J. Biol. Chem. 262:3690-3696(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=1924298; DOI=10.1073/pnas.88.19.8387;
RA Sanni A., Walter P., Boulanger Y., Ebel J.-P., Fasiolo F.;
RT "Evolution of aminoacyl-tRNA synthetase quaternary structure and activity:
RT Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8387-8391(1991).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
CC phenylalanine in mitochondrial translation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000269|PubMed:1924298};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1924298}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 1800 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA94994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02691; AAA34800.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71255; CAA94994.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49219; CAA89167.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11471.1; -; Genomic_DNA.
DR PIR; S54071; YFBYAM.
DR RefSeq; NP_015372.2; NM_001184144.1.
DR AlphaFoldDB; P08425; -.
DR SMR; P08425; -.
DR BioGRID; 36223; 89.
DR DIP; DIP-3901N; -.
DR IntAct; P08425; 1.
DR MINT; P08425; -.
DR STRING; 4932.YPR047W; -.
DR MaxQB; P08425; -.
DR PaxDb; P08425; -.
DR PRIDE; P08425; -.
DR EnsemblFungi; YPR047W_mRNA; YPR047W; YPR047W.
DR GeneID; 856160; -.
DR KEGG; sce:YPR047W; -.
DR SGD; S000006251; MSF1.
DR VEuPathDB; FungiDB:YPR047W; -.
DR eggNOG; KOG2783; Eukaryota.
DR GeneTree; ENSGT00940000158071; -.
DR HOGENOM; CLU_022696_0_1_1; -.
DR InParanoid; P08425; -.
DR OMA; SKSDTYY; -.
DR BioCyc; YEAST:G3O-34202-MON; -.
DR PRO; PR:P08425; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P08425; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0070156; P:mitochondrial phenylalanyl-tRNA aminoacylation; IMP:SGD.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:UniProtKB.
DR Gene3D; 3.30.70.380; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; SSF54991; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00469; pheS_mito; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT CHAIN 18..469
FT /note="Phenylalanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035817"
FT DOMAIN 372..469
FT /note="FDX-ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00778"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162..164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 86
FT /note="K -> E (in Ref. 1; AAA34800)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="D -> H (in Ref. 1; AAA34800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 54829 MW; E728783D76C74C18 CRC64;
MFLNRMMKTR TGLYRLYSTL KVPHVEINGI KYKTDPQTTN VTDSIIKLTD RSLHLKESHP
VGILRDLIEK KLNSVDNTFK IFNNFKPVVT TMENFDSLGF PKDHPGRSKS DTYYINETHL
LRTHTSAHEL ECFQKIRNDS DNIKSGFLIS ADVYRRDEID KTHYPVFHQM EGATIWKRTK
ADVGVKEPMY IEKIREDIRQ VENLLNKENV KITVDDDTIP LKENNPKQEY MSDLEVDLCS
QHLKRSIELI VSEVFNKKIS SMIKNKANNT PKELKVRWIN AYFPWTAPSW EIEVWWQGEW
LELCGCGLIR QDVLLRAGYK PSETIGWAFG LGLDRIAMLL FEIPDIRLLW SRDERFSRQF
SKGLITSFKP YSKHPGSFRD VAFWLPEDKP DIHQVHENDL MEIIRNIAGD LVESVKLVDS
FTHPKTGRKS MCYRINYQSM DRNLTNAEVN TLQDMVCSKL VKEYSVELR
