SYAC_DICDI
ID SYAC_DICDI Reviewed; 946 AA.
AC Q54Y20; Q9U6B5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {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};
GN Name=alaS; ORFNames=DDB_G0277823;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11035802; DOI=10.1073/pnas.220388797;
RA Chihade J.W., Brown J.R., Schimmel P.R., Ribas De Pouplana L.;
RT "Origin of mitochondria in relation to evolutionary history of eukaryotic
RT alanyl-tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12153-12157(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
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: Cytoplasm {ECO:0000255|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: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; AF188717; AAF05592.1; -; mRNA.
DR EMBL; AAFI02000023; EAL68084.1; -; Genomic_DNA.
DR RefSeq; XP_642382.1; XM_637290.1.
DR AlphaFoldDB; Q54Y20; -.
DR SMR; Q54Y20; -.
DR STRING; 44689.DDB0214894; -.
DR PaxDb; Q54Y20; -.
DR EnsemblProtists; EAL68084; EAL68084; DDB_G0277823.
DR GeneID; 8621587; -.
DR KEGG; ddi:DDB_G0277823; -.
DR dictyBase; DDB_G0277823; alaS.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q54Y20; -.
DR OMA; YHHTMFE; -.
DR PhylomeDB; Q54Y20; -.
DR BRENDA; 6.1.1.7; 1939.
DR PRO; PR:Q54Y20; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; ISS:dictyBase.
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; ISS:dictyBase.
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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..946
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000315603"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CONFLICT 18
FT /note="C -> Y (in Ref. 1; AAF05592)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="A -> T (in Ref. 1; AAF05592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 106281 MW; B5A076C7CBF441FB CRC64;
MDVNQIRKTF IDFFREKCEH TFVPSSAVIP HDDPTLLFAN AGMNQFKPIF LGQVNPKSEQ
AKLKRAVNSQ KCIRAGGKHN DLDDVGKDTY HHTFFEMLGN WSFGNYFKKE AITWAWELLT
EVYKLDKERL YVTYFRGDPE KGLEADLEAK NLWLQYLPEE RVLPFGMKEN FWEMGDQGPC
GPCSEIHYDK VEGRDGASFV NADDPTLIEI WNLVFIQYNR EADKSLRPLP QKHVDTGMGL
ERLTSIIQKV PTNYDTDVFM PIFAAIQEVT GYPEPYGGKV GAEDTQQVDM AYRVIADHIR
TLTFSIADGA APSVDGRGQV LRRILRRAVR YGKQKLNAPA GFFSKLVDVV IANFGEFFPE
LRKKPEHIKM VLTREEDMFN KTLEKGIVEF EKMIKKSVNN TLSAENAYFL STCYGFPIDL
TTIMAEEKNY KVDIKGYEGL CEAQSEIDRK RQKEKKVELT LGAEANAWLK NNDIKPTDDS
FKYKQHEIQS VIKAIWNGKE FVDTAPKGTL IGVVLENSNF YAEQGGQIYD IGQLSFIDDQ
KTAFDVKDCK VFGGYVLHIG YLSYECDSLK VGDRVELTVD YTRRSPIMSN HTSTHMVNYA
LKNILGDGID QRGSFVDAQR FRFDFSFGRA ITKDELIKID QIVNDQIFKQ LDVHAKEVGL
ASAKKINGLR AVFGEVYPDP VRVVSVGVPV EQLIENPTNP EWANYSIEFC GGTHLSNTKQ
AELFTITSEE TLGAGVRRIV AVTGSEAASA IELNKELEVR FNNALKLSGS ELAKEIVSLL
DLLKVVTISA SVRMNLVETL KEVQALQRKQ VKEQETILAQ QAQTYLEKTS EELAKSQPKV
FVDLVNFNSN TPLITETIKK IQTKSPMTAI MLISPDEEKG KVTCIGIVPK DSEISKTLTA
NAWVVKVTEV LGGKGGGKVD VAQGVGSKLD KIDEAILVSR EFANAN
