ID C5MG47_CANTT Unreviewed; 803 AA.
AC C5MG47;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 06-MAR-2013, entry version 25.
DE SubName: Full=Glutaminyl-tRNA synthetase;
GN ORFNames=CTRG_05040;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
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DR EMBL; GG692401; EER31310.1; -; Genomic_DNA.
DR RefSeq; XP_002550742.1; XM_002550696.1.
DR GeneID; 8299196; -.
DR KEGG; ctp:CTRG_05040; -.
DR KO; K01886; -.
DR OrthoDB; EOG4FBN23; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth_Ib.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10119; PTHR10119; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; Ribosomal_L25rel; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
SQ SEQUENCE 803 AA; 91467 MW; FFAE418A9B9894F3 CRC64;
MSSNAVISED ELVSLFSKAG FEDKKAKEIV KNKKVASSLY NILDKNTEGN DDKKLALLHQ
LAIHESKNGV VPNHDIIIDS IRKGDLKTTL QVTEGIKYLQ NNEAPIDKEK FNEATGVGIE
ITTEEAKAEI AKYLDSIKSD LETKRYSILA KVLVELKNQP TLKWAPPQIF KPILDEEFLA
RLGPKDERDN MKKKEKKPKT AAKATSNAAA KKNIFDEPEK SMFAEGFLGA LHKPGEEPQK
YPELLEEHRK FINGKVLTRF PPEPNGFLHI GHSKAIMVNF GYAQYNGGKC YLRFDDTNPE
AEEEVYFNSI KEMVSWLGYK PWKITYSSDY FDQLYELAIQ LIKADRAYIC HCTPEEVKVS
RGLKEDGTLG GDRVACKHRS QSIEHNLREF EAMKDGKYAV GEATLRMKQD LESPSPQMWD
LVAYRVLNTP HHRTGDKWKI YPTYDFTHCL VDSFENITHS LCTTEFVLSR ESYEWLCDAL
HVYRPAQREY GRLNLTGTIM SKRKIAKLVN EGYVRGWDDP RLYTLEGIKR RGVPPGAILS
FINTLGVTTA TTNIQSVRFE SAVRNYLDQT TPRLLMVLNP VEVVIDNVDE DFSLDVEIPF
QPGKDEKLMG SRKLTFSKHF YIDASDVRDE PADKEFYRLA PGQPVGLIKV PFNISYKSIE
EKDGKKIVHV NYDEGIKAKP RTYIHWVPKK SAVPVKEVRI YNQLFNSENP SAHPDGYLKD
INPDSEEVLS NAVIEENIKE IITKSPMNVE IPNSEFNIKE NAGNNTVRFQ ALREGYFCLD
KDSKDDSLII NRIVSLKEDA AKN
//