SYA_CANAL
ID SYA_CANAL Reviewed; 969 AA.
AC Q5A8K2; A0A1D8PQ88;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alanine--tRNA ligase {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};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE Flags: Precursor;
GN Name=ALA1 {ECO:0000255|HAMAP-Rule:MF_03133}; Synonyms=SYA1;
GN OrderedLocusNames=CAALFM_C603720WA; ORFNames=CaO19.13169, CaO19.5746;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ALTERNATIVE INITIATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16928688; DOI=10.1074/jbc.m601869200;
RA Huang H.Y., Kuei Y., Chao H.Y., Chen S.J., Yeh L.S., Wang C.C.;
RT "Cross-species and cross-compartmental aminoacylation of isoaccepting tRNAs
RT by a class II tRNA synthetase.";
RL J. Biol. Chem. 281:31430-31439(2006).
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:16928688}.
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 ECO:0000269|PubMed:16928688}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03133, ECO:0000269|PubMed:16928688}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q5A8K2-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=Q5A8K2-2; Sequence=VSP_040237;
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; CP017628; AOW30299.1; -; Genomic_DNA.
DR RefSeq; XP_718082.1; XM_712989.2. [Q5A8K2-1]
DR AlphaFoldDB; Q5A8K2; -.
DR SMR; Q5A8K2; -.
DR STRING; 237561.Q5A8K2; -.
DR PRIDE; Q5A8K2; -.
DR GeneID; 3640285; -.
DR KEGG; cal:CAALFM_C603720WA; -.
DR CGD; CAL0000182169; ALA1.
DR VEuPathDB; FungiDB:C6_03720W_A; -.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q5A8K2; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PRO; PR:Q5A8K2; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IGI:CGD.
DR GO; GO:0005739; C:mitochondrion; IGI:CGD.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IGI:CGD.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IGI:CGD.
DR GO; GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 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; 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 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133,
FT ECO:0000269|PubMed:16928688"
FT CHAIN 9..969
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000402115"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 739
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_040237"
SQ SEQUENCE 969 AA; 108275 MW; 98181CDAA459CB48 CRC64;
MIKTLLRRMS SNTTIPTPNG SNHWTASKVR STFLDYFKKQ QHTYVPSSSV VPHNDPTLLF
ANAGMNQYKP IFLGTVDPAS DFASLKRAAN SQKCIRAGGK HNDLEDVGRD SYHHTFFEML
GNWSFGDYFK KEAIDYSWEL LTKVYGLQED RLYVTYFGGD EKQGLEPDLE AKNFWLKVGV
PEDHILPGSV EDNFWEMGDQ GPCGPCSEIH YDRIGGRNAS ALVNMDDPNV LEVWNVVFIQ
YNREADGNLR TLPNKHIDTG MGFERLVSIL QNKYSNYDTD VFLPIFDKIR EITGVRPYTG
KFGNEDKDGI DTAYRVIADH VRTLTFAICD GGVPNNEGRG YVLRRILRRG SRYVRKYMNY
PIGGFFQQLV DVVIEQNKEI FPEISSGAQD LKEILNEEEL SFAKTLDRGE KLFEQYAIIA
SKTPEQTLSG KDVWRLYDTY GFPVDLTRLM AEEAGLKIDE EGFERAKEES REASKGSGTK
DGKTLVKLDV HALSELDQND AIPKTNDEFK YGLENVKAKV VGIYDGSKFV DSIEDPSIQY
GILLDKTPFY AEQGGQEYDT GKLVIDGKSE FNVANVQVYA GYVLHTGNIV DGKLNVGDEI
IATYDELRRW PIRNNHTGTH ILNFALREVL GDGVDQKGSL VAPEKLRFDF SHKQAVTAKE
LEKIEAISNK YIKNNDKVYY KDVSLTKAKE INGLRAVFGE TYPDPVRVVS IGVSVDDLLA
DPTNTKWHEI SIEFCGGTHV AKTGDIKDLV IIEESGIAKG IRRIVAVTGH DAHHVQKVAN
EFEQEIDNAS SLPFGVAKES KSKELGVALK KLSISVLDKQ RLTEKFNKLD KSIKDNLKAK
QKEETKKTLD VVNNWLNDKE NASSFLVAHV PITANAKAIT EAINLIKKQD KTKSIYLLTG
ETDKVAHGCY VSDEAIAKGI NANELAKAVS ENIGGKAGGK GNIVQGMGDK PQGINTAIEE
VTKLFKEKL
