ID G3TCX9_LOXAF Unreviewed; 985 AA.
AC G3TCX9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN Name=AARS2 {ECO:0000313|Ensembl:ENSLAFP00000011956.3};
GN Synonyms=AARS {ECO:0000256|HAMAP-Rule:MF_03133};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000011956.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000011956.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011956.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000011956.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011956.3};
RG Ensembl;
RL Submitted (JUL-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {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 -!- PTM: ISGylated. {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 RefSeq; XP_003403938.1; XM_003403890.2.
DR AlphaFoldDB; G3TCX9; -.
DR STRING; 9785.ENSLAFP00000011956; -.
DR Ensembl; ENSLAFT00000014276.3; ENSLAFP00000011956.3; ENSLAFG00000014270.3.
DR GeneID; 100655790; -.
DR KEGG; lav:100655790; -.
DR CTD; 57505; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000158246; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; G3TCX9; -.
DR OMA; DTEACCG; -.
DR OrthoDB; 3639120at2759; -.
DR TreeFam; TF300737; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
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:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:Ensembl.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 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 NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF8; ALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
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 Metal-binding {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}; Reference proteome {ECO:0000313|Proteomes:UP000007646};
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}; Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03133};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03133}.
FT DOMAIN 37..792
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 985 AA; 106948 MW; 2873FFA3E9CE1076 CRC64;
MVASVAAAAG RLRRALGRSP SWRGSSRRLL SSEPPPAPAT AVRDAFLSFF RDRHGHRLVP
SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR RVANSQKCVR AGGRHNDLED
VGRDLSHHTF FEMLGSWAFG GEYFKKEACS MAWELLTQVY GIPEDRLWVS YFGGDPKARL
DPDLETRDIW LSLGVPASRV LSLGPQENFW EMGDTGPCGP CTEIHYDLAG GTGAPQLVEL
WNLVFMQHNR ETDGSLQPLP QRHVDTGMGL ERLVAVLQGR RSTYDTDLFS PLLNAIHQGC
GAPPYLGRVG AADEGRVDTA YRVVADHIRM LSVCIADGVS PGMSGAPLVL RRILRRAVRF
ATEILRAPPG FLGSLVPVVV ETLGDIYPEL QKNSAQIASL VSDDEAAFLA SLQRGRQIID
RTLRRLGPSD MFPAEVAWSL SLSGHLGLPL DLVELMLEEK GVQLDSAGLE RLAREEAQHR
AQQAEPARKQ GMRLDVHALG ELRRQGVPLT DDSPKYNYFL RPTGGYEFRA CEAQVLQLYT
EDGTAVTSIG GGQRCGLLLD RTNFYAEQGG QASDRGYLVR AEQQDVLFPV ARAQVCGGFI
LHEAVAPECL QVGDQVQLHV DKAWRLGCME KHTATHLLNW ALRQALGPGT EQRGSHLNPE
RLRLDVATQA PLTPQQLQAV EGAVQEAVGQ DEPVYTDEVA LALTAQVPGL RSLDEVYPDP
VRVVSVGVPV AQALDPASQA ALQTSVELCC GTHLLRTGAV GDLVIIGERQ LAKGTTRLLA
ITGEQAQQAR EVGQSLAQEV KAAAERLSRG SQDVVEARRL SKHMGRLTDA VDTAVMPQWQ
RRELQATLKV LQRRANTAIR KLETGQAAKK TQELLERHTE GPLIVDTVPA ESLSVLVKVV
RQLCEQAPST SVLLLSPQPL GNVLCACQVA QGATPAFTAE AWALAVCSHM GGKAWGTQVV
AQGTGSTADL ETALSTARAY ALTQL
//