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Database: UniProt
Entry: G3TCX9_LOXAF
LinkDB: G3TCX9_LOXAF
Original site: G3TCX9_LOXAF 
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
//
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