SYAC_DROME
ID SYAC_DROME Reviewed; 966 AA.
AC Q9VLM8; Q8T9K4; Q9U6B4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {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, ECO:0000312|FlyBase:FBgn0027094};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
GN Name=AlaRS {ECO:0000312|FlyBase:FBgn0027094};
GN Synonyms=Aats-ala {ECO:0000255|HAMAP-Rule:MF_03133,
GN ECO:0000312|FlyBase:FBgn0027094}, alaS {ECO:0000303|PubMed:11035802};
GN ORFNames=CG13391 {ECO:0000312|FlyBase:FBgn0027094};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11035802; DOI=10.1073/pnas.220388797;
RA Chihade J.W., Brown J.R., Schimmel P.R., Ribas De Pouplana L.;
RT "Origin of mitochondria in relation to evolutionary history of eukaryotic
RT alanyl-tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12153-12157(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged tRNA(Ala) via its editing domain.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-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-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF05593.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF188718; AAF05593.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF52657.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64737.1; -; Genomic_DNA.
DR EMBL; AY069255; AAL39400.1; -; mRNA.
DR RefSeq; NP_523511.2; NM_078787.4.
DR RefSeq; NP_995656.1; NM_205934.3.
DR AlphaFoldDB; Q9VLM8; -.
DR SMR; Q9VLM8; -.
DR BioGRID; 60280; 1.
DR IntAct; Q9VLM8; 3.
DR STRING; 7227.FBpp0079326; -.
DR PaxDb; Q9VLM8; -.
DR PRIDE; Q9VLM8; -.
DR EnsemblMetazoa; FBtr0079721; FBpp0079326; FBgn0027094.
DR EnsemblMetazoa; FBtr0079722; FBpp0089366; FBgn0027094.
DR GeneID; 34156; -.
DR KEGG; dme:Dmel_CG13391; -.
DR UCSC; CG13391-RA; d. melanogaster.
DR CTD; 34156; -.
DR FlyBase; FBgn0027094; AlaRS.
DR VEuPathDB; VectorBase:FBgn0027094; -.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q9VLM8; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q9VLM8; -.
DR BioGRID-ORCS; 34156; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 34156; -.
DR PRO; PR:Q9VLM8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027094; Expressed in eye disc (Drosophila) and 38 other tissues.
DR ExpressionAtlas; Q9VLM8; baseline and differential.
DR Genevisible; Q9VLM8; DM.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
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:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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_sf.
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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..966
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000402114"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CONFLICT 489
FT /note="E -> D (in Ref. 4; AAL39400)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="T -> A (in Ref. 4; AAL39400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 966 AA; 107741 MW; B1B63A7A8FB87B6E CRC64;
MKLLTAKEVR NAYLDFFKEQ KHIYVHSSST IPLDDPTLLF ANAGMNQFKP IFLGTADPNS
EMSKWVRVAN TQKCIRAGGK HNDLDDVGKD VYHHTFFEML GNWSFGDYFK KEICSWAWEF
LTQRLALPKD RLYVTYFGGD AASGLEPDLE CKQMWLDLGL KPEHILPGSM KDNFWEMGET
GPCGPCSELH FDRIGGRSVP ELVNMDDPDV LEIWNLVFIQ YNRESDGSLK QLPKKHIDCG
MGFERLVSVI QNKRSNYDTD LFVPLFDAIQ AGTGAPPYQG RVGADDVDGI DMAYRVLADH
ARTITIALAD GGTPDNTGRG YVLRRILRRA VRYATEKLNA KPGFFATLVN TVVDLLGDAF
PEVKKDPQHI IDIINEEELQ FLKTLTRGRN LLNRTIEKLG NQTTIPGDVA WRLYDTYGFP
VDLTQLMAEE KSLKIDMDGY EAAKHNSYVL SQGKGASKIE EINLDVHAIS QLQEQGVPPT
NDTFKYKYEA VSDERDSAYN YGVCNSKIVA LRFENQFVNE ITSGQKAGIV LDKTNFYAES
GGQIYDQGAL VKVNDEANEF LVDRVYNRGG YILHIGVVEG TLKVGDELEL HIDVERRWLT
MKNHSATHAL NHCLLQVLGK DTEQKGSLVV PEKLRFDFNS KAAMTIEQVS KTEQLTKEMV
YKNVPIYAKE SKLALAKKIR GLRSVFDEVY PDPVRVISFG VPVDELEQNP DSEAGEQTSV
EFCGGTHLRR SGHIMDFVIS SEEAIAKGIR RIVALTGPEA LKALKKSEAF EQEIVRLKAT
IDNDKSGKDS KSHVKEIVEL TEQISHATIP YVKKDEMRNL LKGLKKTLDD KERALRAAVS
VTVVERAKTL CEANPNATVL VEQLEAFNNT KALDAALKQV RSQLPDAAAM FLSVDADSKK
IFCLSSVPKS AVEKGLKANE WVQHVSATLG GKGGGKPESA QASGTNYEKV DEIVQLASKF
AQSKLS
