SYAM_DROME
ID SYAM_DROME Reviewed; 1012 AA.
AC Q9VRJ1; Q9U6B6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alanine--tRNA ligase, mitochondrial {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:0000303|PubMed:11532948};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000303|PubMed:11532948};
DE Flags: Precursor;
GN Name=AlaRS-m {ECO:0000312|FlyBase:FBgn0028962};
GN Synonyms=Aats-ala-m {ECO:0000255|HAMAP-Rule:MF_03133}, alaS;
GN ORFNames=CG4633 {ECO:0000312|FlyBase:FBgn0028962};
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).
RN [5]
RP FUNCTION.
RX PubMed=11532948; DOI=10.1093/emboj/20.17.4846;
RA Lovato M.A., Chihade J.W., Schimmel P.;
RT "Translocation within the acceptor helix of a major tRNA identity
RT determinant.";
RL EMBO J. 20:4846-4853(2001).
RN [6]
RP FUNCTION.
RX PubMed=15053877; DOI=10.1016/s1097-2765(04)00125-x;
RA Lovato M.A., Swairjo M.A., Schimmel P.;
RT "Positional recognition of a tRNA determinant dependent on a peptide
RT insertion.";
RL Mol. Cell 13:843-851(2004).
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, ECO:0000269|PubMed:11532948,
CC ECO:0000269|PubMed:15053877}.
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: Mitochondrion {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}.
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DR EMBL; AF188716; AAF05591.1; -; mRNA.
DR EMBL; AE014296; AAF50804.1; -; Genomic_DNA.
DR EMBL; AY128439; AAM75032.1; -; mRNA.
DR EMBL; BT001744; AAN71499.1; -; mRNA.
DR RefSeq; NP_523932.2; NM_079208.3.
DR AlphaFoldDB; Q9VRJ1; -.
DR SMR; Q9VRJ1; -.
DR IntAct; Q9VRJ1; 3.
DR STRING; 7227.FBpp0076871; -.
DR PaxDb; Q9VRJ1; -.
DR PRIDE; Q9VRJ1; -.
DR EnsemblMetazoa; FBtr0077168; FBpp0076871; FBgn0028962.
DR GeneID; 38595; -.
DR KEGG; dme:Dmel_CG4633; -.
DR UCSC; CG4633-RA; d. melanogaster.
DR CTD; 38595; -.
DR FlyBase; FBgn0028962; AlaRS-m.
DR VEuPathDB; VectorBase:FBgn0028962; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000158246; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q9VRJ1; -.
DR OMA; PVVPFCD; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q9VRJ1; -.
DR BRENDA; 6.1.1.7; 1994.
DR BioGRID-ORCS; 38595; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38595; -.
DR PRO; PR:Q9VRJ1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0028962; Expressed in mouthpart and 24 other tissues.
DR Genevisible; Q9VRJ1; DM.
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; ISS:FlyBase.
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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 2.
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; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CHAIN 25..1012
FT /note="Alanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000402119"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 660
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CONFLICT 477
FT /note="S -> N (in Ref. 1; AAF05591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 113104 MW; 64A77466EF32FEC5 CRC64;
MYNSAKQLQR VLTAREIRKT FLDHFTVNHG HKFVRSSPVV PFCDPTVAFV NAGMNQFKSV
FLGTAAAPHK RVVNSQKCVR VGGKHNDLSV VGTDGYHHTF FEMLGNWSFG DYFKREACAM
ALELLRGPYN IDPGRLYVTY FAGDKVLGIP ADLECFEIWR SLGFPASRIL PFGCADNFWE
MGATGPCGPC TEIHIDHRPD LGSVEQRAKL VNAGRSDLTE LWNLVFIQYN RHADGSISQL
PAHHVDTGMG FERLTAVLQN KSSNYDTDLF TPIFDGIQQA AKTPVYSGSF PDGGNAAVLD
TSYRILADHA RMVTACLADG MLPDQNQKLR RVLRKALNIS EHVFAHDKLL TQLVPIVVET
LGEAYPEMAA KQQAVIDLIC HEQEVYKNLR ESSSKAFAEV LMEFPNLDDI DLMECPGFVP
AYRELQMQRC KFSNNTIPGD FLYKLTDTYG LTEESFLKLA ELENMNCDLE RYRAEVSLAK
LKAKGNQRET AGGSLCDLAT EQRIAEAQAM LTKRLTPTDN SHKYTYSFDK ESDSYQIPPL
KTRVLGMLLN DAEVSRTQGS RIQQPFTDLI SIVTAGSNFY YESGGQQSDG GKILVSNHQQ
PDHPHSLDVI GVKHLNDCVV HICKLSSPTD AFQLAIGDEV ELQVDAQQRQ LNTCHHTATH
LLNAAIRSLF KKVTYQVSSS VSSDQCKLEL GLLGKRIQKT DVQLIEDLIN RVICSAAPVE
VQLLSAAEVL EQNDITMVPG EVYPEQGLRL VNVESPELQL SSKELCCGTH ATNTSELSCF
CIVNLKQTNR ARFAFTAVAG QAAENVLKTA ALLRHRVDLL EKQFQTDKLT NATEAELQTI
RHNMLHTDIK LPYAFKMDTL ERITEMLKRI KDSSRTTLKE FVDVEMRTLL QEKPLDTHPF
ILHYITSSAL VEEIPLQRAT KLCPDRPILV ISVCDSVVKA RCCVPEKCIT EKFNASAWLQ
SFADTFNGQI AAPKGQNPQA VCNMKGRRVS NLFEEQLEQA MSKAHAYAKL YL
