(data stored in ACNUC16935 zone)

SWISSPROT: SYA_EMENI

ID   SYA_EMENI               Reviewed;         961 AA.
AC   Q5AQL1; C8VLV5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_03133};
DE            EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE            Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
GN   Name=ala1; ORFNames=AN9419;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged tRNA(Ala) via its editing domain.
CC       {ECO:0000255|HAMAP-Rule:MF_03133}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP-
CC       Rule:MF_03133}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03133};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03133}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_03133}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA66836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACD01000175; EAA66836.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF84773.1; -; Genomic_DNA.
DR   RefSeq; XP_868801.1; XM_863708.1.
DR   ProteinModelPortal; Q5AQL1; -.
DR   STRING; 162425.CADANIAP00008005; -.
DR   PRIDE; Q5AQL1; -.
DR   EnsemblFungi; CADANIAT00008005; CADANIAP00008005; CADANIAG00008005.
DR   EnsemblFungi; EAA66836; EAA66836; AN9419.2.
DR   GeneID; 3684011; -.
DR   KEGG; ani:AN9419.2; -.
DR   HOGENOM; HOG000156964; -.
DR   InParanoid; Q5AQL1; -.
DR   KO; K01872; -.
DR   OMA; FEMMAHH; -.
DR   OrthoDB; EOG092C0P21; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5AQL1.
DR   SWISS-2DPAGE; Q5AQL1.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding;
KW   Zinc.
FT   CHAIN         1    961       Alanine--tRNA ligase.
FT                                /FTId=PRO_0000402116.
FT   METAL       604    604       Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
FT   METAL       608    608       Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
FT   METAL       723    723       Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
FT   METAL       727    727       Zinc. {ECO:0000255|HAMAP-Rule:MF_03133}.
SQ   SEQUENCE   961 AA;  107306 MW;  249DFD6BFE0F9727 CRC64;
     MASNLQSQPK WTSKLVRDTF LQYFQGKGHT FVASSPVAPL SDPTLLFTNA GMNQFKSIFL
     GTVNPNSDFA QLKSAVNSQK CIRAGGKHND LDDVGKDSYH HTFFEMLGNW SFGDYFKKEA
     IQYSWELLTQ VYGLDPGRLY VTYFEGNKEG GLQPDLEAKA LWKAVGVPED HILPGNMKDN
     FWEMGDQGPC GPCSEIHYDR IGGRNAASLV NQDDPNVLEI WNNVFIQYNR ENDGSLRSLP
     NKHVDTGMGF ERLVSVLQDK SSNYDTDVFG PIFQTIQVIT GAREYQGRFG TDDSDGIDTA
     YRVVADHVRT LMFAISDGVV PNNEGRGYVI RRVLRRGARY ARKYFNVEIG SFFSKIVPTV
     VEQLGDMFPE LKQKQQDVIE ILNEEEISFA KTLDRGERQF EQYAQQAKTA GDHKLHGADV
     WRLYDTFGFP VDLTRIMAEE RGLEIDDRQF EEARHKAKEA SKGQKKTTTG SVKLDVHDLG
     KLEKMNGVPK TDDSAKFEIG NVTAQIKAIY HGKTFHSSTQ NLDDSEQIGI ILDRTNFYAE
     QGGQENDTGR IVIDGQAELE VVDVQQYAGY VLHTGYMKYG SFKVDDTVIC EYDELRRWPI
     RNNHTGTHIL NFALRGVLGD GIEQKGSLVS AEKLRFDFSH KSPVTDVELV KIEDLSTQYI
     RRNCLVYSKE VPLSIARNIA GVRAVFGETY PDPVRVVSVG AELDEILKNV EDPRWADFSI
     EFCGGTHVQK TGDIKDLVIL EESGIAKGIR RIIAVTGEDA HEVQRLAEEF EKRLNHLEAM
     PSGSAKEQNA KQIQVELNQL SISAVQKSRF RERFTQINKK IIDEQKAQQK LESKKAVESI
     TSYFAAPENA NKSWLIAKLP ISANAKAVSE CLTYVKTKLA DKMVYVLASS LEDGRVAHGC
     YVPKAISDQG ASASEWSSAV SRAVGGKAGG KGPTSIGNGI NPEKVDDAVD LASEYLSKFK
     L
//

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