ID M3YMB1_MUSPF Unreviewed; 1007 AA.
AC M3YMB1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ENSMPUP00000012468.1,
GN ECO:0000313|RefSeq:XP_004739847.1};
GN Synonyms=AARS {ECO:0000256|HAMAP-Rule:MF_03133};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012468.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012468.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004739847.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004739847.1};
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 -!- 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 Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}.
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; AEYP01006061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004739847.1; XM_004739790.3.
DR STRING; 9669.ENSMPUP00000012468; -.
DR Ensembl; ENSMPUT00000012670.1; ENSMPUP00000012468.1; ENSMPUG00000012562.1.
DR GeneID; 101683978; -.
DR KEGG; mpuf:101683978; -.
DR CTD; 57505; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000158246; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR OMA; HVFVQLM; -.
DR OrthoDB; 3639120at2759; -.
DR Proteomes; UP000000715; Unplaced.
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:UP000000715};
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 988..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1007
FT /note="Polar residues"
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 1007 AA; 109618 MW; ACB714D311D6E603 CRC64;
MAVSMAAAAG RLRRAIRRSP LWVSPSRQPL SSEPPPAQAT AVRDAFLNFF RDRHGHRLVP
SASVRPRGDP SLLFVNAGMN QFKPIFLGTV NPRSEMAGFR RVANSQKCVR AGGRHSDLED
VGRDLSHHTF FEMLGNWAFG GEYFKEEACS MAWELLTQVY GIPEDRLWVS YFGGDPNAGL
DPDLESRDIW LSLGVPASHV LSFGPQENFW EMGDTGPCGP CTEIHYDLTG RVGAPQLVEL
WNLVFIQHNR EADGSLQPLP QRHVDTGMGL ERLVAVLQGT RSTYDTDLFS PLLKAIHQGC
GAPPYLGRVG AADEGRTDMA YRVVADHIRT LSICIADGVY PGMSGAPLVL RRILRRAVRF
STEVLRAPPG LLSSLVPIVV ETLGDAYPEL QKNSAQIASL ISEDEAAFLA SLQRGRRIID
RTLRRLGPAK LFPAEVAWSL SLSGNLGLPL DLLELMLEEK GVQLDSAGLA RLAQEDAQHR
SQQAEPVQEQ GLQLSVHALG ELQRRGVPPT DDSPKYNYSL RPSGGYEFST CEAQVLQLYT
EDGTAVASVG KGQRFGLLLD KTNFYAEQGG QASDRGYLTR VDQEDVLFPV ARAQVCGGFI
LHEAVAPEDL KVGDQVQLHV DEAWRLGCMK KHTATHLLSW ALRQALGPGT EQRGSHLNPE
RLRFDVATQA PLTSQQLRAV EGTVRDAVAQ DKPVYVEDVA LARTAHVPGL RCLDEVYPDP
VRVVSVGVPV AHALDPGSQA ALQTSVELCC GTHLLRTGAI GDLVIVGERQ LTRGTTRLLA
VTGEQAQQAR EVGQNLAQEV EAATERLSQG SKDVVAAQRL SKDMGRLTDA VDLAMMPQWQ
RRELQATLKG LQRRANTAVR KLELGQAAQK TQELLQRHSQ GPLIVDTVAA ESLSVLVKVV
RQLCERVPGT SVFLLSPQQL GHVLCACQVA QSATPAFTAE AWALAVCSHM GGKAWGSQVA
ARGAGTTTDL EAVLSTARAY ALDRLQPSSP TDLHRLHRQQ TGPGQEL
//
