ID F1QBG7_DANRE Unreviewed; 433 AA.
AC F1QBG7; A0A8M1N8I8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN Name=aars1 {ECO:0000313|Ensembl:ENSDARP00000071166,
GN ECO:0000313|RefSeq:NP_001035124.2,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-3663};
GN Synonyms=AARS {ECO:0000256|HAMAP-Rule:MF_03133}, aars
GN {ECO:0000313|RefSeq:NP_001035124.2}, im:7146712
GN {ECO:0000313|RefSeq:NP_001035124.2}, si:ch211-223o1.6
GN {ECO:0000313|RefSeq:NP_001035124.2}, wu:fc48h07
GN {ECO:0000313|RefSeq:NP_001035124.2}, zgc:113920
GN {ECO:0000313|RefSeq:NP_001035124.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000071166};
RN [1] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=16109975;
RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL Genome Res. 15:1307-1314(2005).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000071166}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000071166};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000071166, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000071166};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=25534026; DOI=10.1093/molbev/msu395;
RA Petit D., Teppa E., Mir A.M., Vicogne D., Thisse C., Thisse B., Filloux C.,
RA Harduin-Lepers A.;
RT "Integrative view of alpha2,3-sialyltransferases (ST3Gal) molecular and
RT functional evolution in deuterostomes: significance of lineage-specific
RT losses.";
RL Mol. Biol. Evol. 32:906-927(2015).
RN [5] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=27895053; DOI=10.1242/bio.020974;
RA Capon S.J., Baillie G.J., Bower N.I., da Silva J.A., Paterson S.,
RA Hogan B.M., Simons C., Smith K.A.;
RT "Utilising polymorphisms to achieve allele-specific genome editing in
RT zebrafish.";
RL Biol. Open 6:125-131(2017).
RN [6] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [7] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=28934368; DOI=10.1371/journal.pone.0185317;
RA Waldron A.L., Cahan S.H., Francklyn C.S., Ebert A.M.;
RT "A single Danio rerio hars gene encodes both cytoplasmic and mitochondrial
RT histidyl-tRNA synthetases.";
RL PLoS ONE 12:E0185317-E0185317(2017).
RN [8] {ECO:0000313|RefSeq:NP_001035124.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RX PubMed=30124830;
RA Weterman M.A.J., Kuo M., Kenter S.B., Gordillo S., Karjosukarso D.W.,
RA Takase R., Bronk M., Oprescu S., van Ruissen F., Witteveen R.J.W.,
RA Bienfait H.M.E., Breuning M., Verhamme C., Hou Y.M., de Visser M.,
RA Antonellis A., Baas F.;
RT "Hypermorphic and hypomorphic AARS alleles in patients with CMT2N expand
RT clinical and molecular heterogeneities.";
RL Hum. Mol. Genet. 27:4036-4050(2018).
RN [9] {ECO:0000313|RefSeq:NP_001035124.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001035124.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. Interacts with ANKRD16; the interaction is direct.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_03133}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_03133}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03133}.
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DR EMBL; BX571681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001035124.2; NM_001040035.2.
DR Ensembl; ENSDART00000076695; ENSDARP00000071166; ENSDARG00000069142.
DR Ensembl; ENSDART00000076695.6; ENSDARP00000071166.4; ENSDARG00000069142.8.
DR GeneID; 324940; -.
DR KEGG; dre:324940; -.
DR AGR; ZFIN:ZDB-GENE-030131-3663; -.
DR CTD; 16; -.
DR ZFIN; ZDB-GENE-030131-3663; aars1.
DR HOGENOM; CLU_004485_0_0_1; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000000437; Alternate scaffold 18.
DR Proteomes; UP000000437; Chromosome 18.
DR Bgee; ENSDARG00000069142; Expressed in somite and 28 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00673; AlaRS_core; 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 NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF36; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_03133};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03133};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1QBG7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03133};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03133}.
FT DOMAIN 5..433
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 433 AA; 48788 MW; FB3E870523B18292 CRC64;
MDSSLTAAQI REKFIDFFRR HEHQYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS
HPMARLRRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KHLACKMALE
LLTQEFGIPI ERLYVTYFGG HADAGLEPDL ECKQIWLDLG MEESRILPGS MKDNFWEMGD
TGPCGPCSEI HYDRIGGRDA AHLVNMDDPN VLEIWNLVFI QFNRESETVL KPLPKKSIDT
GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARAYT GKVGAEDTDG IDMAYRVLAD
HARTITIALS DGGRPDNTGR GYVLRRILRR AVRYSHEKLG AQRGFFASLV DVVVKSLGDA
FPELRKDPDM VKDIINEEEA QFLKTLSRGR RILDRKIQSL GESTTIPEGM LFTGASSLHL
HINGEQEVGD RVK
//
