ID A0A0Y9Y3U7_PLABE Unreviewed; 1218 AA.
AC A0A0Y9Y3U7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_03133};
GN Name=AlaRS {ECO:0000313|EMBL:CXI69622.1};
GN ORFNames=PBK173_000309300 {ECO:0000313|EMBL:CXI69622.1},
GN PBNK65E_000301400 {ECO:0000313|EMBL:SCN27024.1}, PBNK65NY_000301000
GN {ECO:0000313|EMBL:SCM24242.1}, PBSP11A_000301000
GN {ECO:0000313|EMBL:SCO63447.1}, PBSP11RLL_000301400
GN {ECO:0000313|EMBL:SCO61469.1};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:CXI69622.1, ECO:0000313|Proteomes:UP000069549};
RN [1] {ECO:0000313|EMBL:CXI69622.1, ECO:0000313|Proteomes:UP000069549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K173 {ECO:0000313|EMBL:CXI69622.1,
RC ECO:0000313|Proteomes:UP000069549}, NK65 ny
RC {ECO:0000313|EMBL:SCM24242.1, ECO:0000313|Proteomes:UP000516480},
RC NK65e {ECO:0000313|EMBL:SCN27024.1,
RC ECO:0000313|Proteomes:UP000220214}, SP11 Antwerpcl1
RC {ECO:0000313|EMBL:SCO63447.1, ECO:0000313|Proteomes:UP000219860}, and
RC SP11 RLL {ECO:0000313|EMBL:SCO61469.1,
RC ECO:0000313|Proteomes:UP000219974};
RG Pathogen Informatics;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_03133}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}.
CC Cytoplasm {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 -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT160031; CXI69622.1; -; Genomic_DNA.
DR EMBL; LT608147; SCM24242.1; -; Genomic_DNA.
DR EMBL; LT614637; SCN27024.1; -; Genomic_DNA.
DR EMBL; LT608275; SCO61469.1; -; Genomic_DNA.
DR EMBL; LT608259; SCO63447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Y9Y3U7; -.
DR VEuPathDB; PlasmoDB:PBANKA_1143600; -.
DR OMA; QYNKDEK; -.
DR Proteomes; UP000069549; Chromosome 11.
DR Proteomes; UP000219860; Chromosome 11.
DR Proteomes; UP000219974; Chromosome 11.
DR Proteomes; UP000220214; Chromosome 11.
DR Proteomes; UP000516480; Chromosome 11.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 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:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 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; 2.
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}; Cytoplasm {ECO:0000256|HAMAP-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 Mitochondrion {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};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03133}; Signal {ECO:0000256|SAM:SignalP};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03133}; Zinc {ECO:0000256|HAMAP-Rule:MF_03133}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1218
FT /note="Alanine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014242982"
FT DOMAIN 190..1027
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 984
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT BINDING 988
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ SEQUENCE 1218 AA; 141346 MW; B1E21FF0C625B658 CRC64;
MIICSFIILF LYIFLNTNKQ VTLGIRINKA FKITDKNQPH KKKNDSSNSY VPNKILFIDE
KKKNNLPVHV KRVKKRYLKS REQINEYMLF NHINPKLQNI GFATKYTCKY NLNRGHINSI
FNFIYLLKGN IPKKHFITNT HKMNKSDKTS LKRYDIENEE TGYLHTDKNN ENSEINGQNI
GNKQNEYKYM TSEQVRNNFI NYFKNKDHTI VDSASVIPYN DNTLLFTNAG MNQFKKIFLG
NVDKNSDLGK LKRCVDTQKC IRAGGKHNDL DDVGKDVYHH TFFEMLGNWS FGDYFKEESI
EYAWDLLTNV YKINPNRLYV TYFGGDKNLP SCPPDLEAKK IWSKYLDEKR ILPFGMKDNF
WEMAETGPCG PCSEIHYDRI GNRDASDLVN KDDPSVLEIW NIVFMQYNKD ENKNMNKLPS
PCIDTGMGLE RITSILQNVQ SNYDTDLFTP IFKQIKEIFN DNIPSYQGKI NEQDPDKIDY
AYRVISDHIR CATIAISDGC IPSNEGRNYV IRRIIRRAIR VGKQVFNIKS NVLWFYKLVD
SVCKILGNCF KDLQNEEKVN YIKNVIMQEE LIFNKTLEKG VDQFNKIIKR CHQNPSNNNN
LFSGKDAFDL YTSYGFPIDL IEIMCEEKSV KLNMEEFNTL FKKHQLVSDT NNFKINKVID
LPVEKAHDIK CKYNVLPTID YHKYNWNNTF EVPKSKEENK NNLRLKSSVQ IIYDGNFLDE
IMHTDDEAKE PLSCVKVENK QKKYALILKE TNFYYENGGQ IYDTGFIQNE SMKFQVLNVQ
KMSDYILHIG VLLSGCIKKN DIIEAVVDFE RRKLIACNHT ATHLLNFSLR KVLADQMNQK
KNKCDNKDEN KKVSLEDSNT IKNKLEENSS CNNNSNGSSI FNCEQKGSLV DDEKLRFDFS
FIQNINTDVL NKIETEINNI VKEELDVSVK TMDLTESKKI KGIRAIFEED YSDKVNVVFI
SKNADNVLNN LDVNYTYLCS IELCGGTHIG NTKYIKEFII TSEESIGKGI HRINAVTNKK
AEEINKKFDD LVSKYKHVFD DPNENKLTDV QNYKRILKED KFLPLIKKNK ILEDLEIIEK
DIVEKKKNAQ KELFNKAMRM GKLYATENKD NVLLDIKLFT EINGNQKVLE KVGQAYNKAN
KNLSYFFIIH DENNTYCVLE IRDSLKCKEI QAETFMKQVM GSVEGHSGGG KNKAFGSAEK
DKGTAIKQAA EEVIKKYL
//
