ID   SYG2_YEAST              Reviewed;         618 AA.
AC   Q06817;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Glycyl-tRNA synthetase 2;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycine--tRNA ligase 2;
DE            Short=GlyRS 2;
DE            Short=GlyRS2;
GN   Name=GRS2; OrderedLocusNames=YPR081C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313271; 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.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   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.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   FUNCTION.
RX   PubMed=10874035; DOI=10.1074/jbc.M003416200;
RA   Turner R.J., Lovato M., Schimmel P.;
RT   "One of two genes encoding glycyl-tRNA synthetase in Saccharomyces
RT   cerevisiae provides mitochondrial and cytoplasmic functions.";
RL   J. Biol. Chem. 275:27681-27688(2000).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 2290 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- CAUTION: GRS1, which appears to be a duplication of GRS2, is
CC       necessary and sufficient for both mitochondrial and cytoplasmic
CC       glycyl-tRNA synthetase activities, suggesting that GRS2 may not be
CC       essential.
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DR   EMBL; U51033; AAB68130.1; -; Genomic_DNA.
DR   PIR; S69067; S69067.
DR   RefSeq; NP_015406.1; -.
DR   HSSP; P56206; 1B76.
DR   IntAct; Q06817; 1.
DR   PeptideAtlas; Q06817; -.
DR   Ensembl; YPR081C; Saccharomyces cerevisiae.
DR   GeneID; 856196; -.
DR   GenomeReviews; U00094_GR; YPR081C.
DR   KEGG; sce:YPR081C; -.
DR   NMPDR; fig|4932.3.peg.6543; -.
DR   CYGD; YPR081c; -.
DR   SGD; S000006285; GRS2.
DR   HOGENOM; Q06817; -.
DR   OMA; Q06817; INENDSR.
DR   BRENDA; 6.1.1.14; 250.
DR   NextBio; 981387; -.
DR   GermOnline; YPR081C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR002315; tRNA-synt_gly.
DR   InterPro; IPR018160; tRNA-synth_gly_a2dimer_C.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   PANTHER; PTHR10745; tRNA-synt_gly; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01043; TRNASYNTHGLY.
DR   TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    618       Glycyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000073006.
SQ   SEQUENCE   618 AA;  71018 MW;  91D36F04D1AF7F38 CRC64;
     MPLMSNSERD KLESTLRRRF FYTPSFEIYG GVSGLFDLGP PGCQLQNNLI RLWREHFIME
     ENMLQVDGPM LTPYDVLKTS GHVDKFTDWM CRNPKTGEYY RADHLIEQTL KKRLLDKDVN
     PQDMKNMEKI LTTIDGFSGP ELNLVMQEYN INDPVTNDVL DALTSFNLMF ETKIGASGQL
     KAFLRPETAQ GQFLNFNKLL EINQGKIPFA SASIGKSFRN EISPRSGLLR VREFLMAEIE
     HFVDPLNKSH AKFNEVLNEE IPLLSRRLQE SGEVQLPVKM TIGEAVNSGM VENETLGYFM
     ARVHQFLLNI GINKDKFRFR QHLKNEMAHY ATDCWDGEIL TSYGWIECVG CADRAAFDLT
     VHSKKTGRSL TVKQKLDTPK ERTEWVVEVN KKFFGSKFKQ KAKLIESVLS KFSQDELIRR
     HEELEKNGEF TCQVNGQIVK LDSSLVTIKM KTTLQHIREY IPNVIEPSFG LGRIIYCIFD
     HCFQVRVDSE SRGFFSFPLQ IAPIKVFVTT ISNNDGFPAI LKRISQALRK REIYFKIDDS
     NTSIGKKYAR NDELGTPFGI TIDFETIKDQ TVTLRERNSM RQVRGTITDV ISTIDKMLHN
     PDESDWDKST FGLSPVKI
//