ID A0A0E0L9X4_ORYPU Unreviewed; 951 AA.
AC A0A0E0L9X4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Probable alanine--tRNA ligase, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03134};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_03134};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_03134};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_03134};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G08850.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC06G08850.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC06G08850.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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_03134}.
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_03134};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03134};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03134};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03134}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03134}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03134}.
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_03134}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}.
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DR AlphaFoldDB; A0A0E0L9X4; -.
DR EnsemblPlants; OPUNC06G08850.2; OPUNC06G08850.2; OPUNC06G08850.
DR Gramene; OPUNC06G08850.2; OPUNC06G08850.2; OPUNC06G08850.
DR HOGENOM; CLU_004485_1_1_1; -.
DR Proteomes; UP000026962; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 6.10.250.550; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR HAMAP; MF_03134; Ala_tRNA_synth_plantC; 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; IPR027522; Ala_tRNA_synth_plant.
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 NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 2.
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_03134};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03134};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|HAMAP-
KW Rule:MF_03134}; Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03134};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03134};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03134};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|HAMAP-Rule:MF_03134};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03134}; Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03134}; Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03134}; Zinc {ECO:0000256|HAMAP-Rule:MF_03134}.
FT DOMAIN 96..777
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 40..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 793..827
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 69..89
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_03134"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 738
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
SQ SEQUENCE 951 AA; 103710 MW; CC0809C9046745AF CRC64;
MEAAALLSPT AATSRPLPIL STAPAAHRLH VLLPLSGRRR LRSSPRPRGS LVCAGDGVAR
RRGSSRERGV LVRSSSSSAS VESATQEVGA ASSGEWSGDA IRRRFLDFYA ARGHKILPSS
SLVPDDPTVF LTIAGMLQFK PIFLGKEPRR VPCATTSQKC IRTNDIENVG RTSRHQTFFE
MLGNFSFGDY FKKEAITWAW ELTTKEFGLP SERLWISVFQ DDDEAFSIWH NEVGVPKERI
KRLGEDDNFW TSGATGPCGP CSEIYYDFYP ERGSSDADLG DDSRFIEFYN LVFMQYNKKD
DGSLEPLKQK NIDTGMGLER MARILQKVPN NYETDLIFPI IEKAASMALV SYTTADDAMK
TNLKIIGDHM RAVVYLISDG VIPSNIGRGY VVRRLIRRVV RTGRLIGIRG DGHGNSEGAF
LPSLAEVAIS LSTEIDPDVE SRRKSILGEL QREELRFVQT LERGEKLLDE LLDEALSSAG
NNGGKPCLSG KDVFLLYDTY GFPVEITAEI AGERGVIVDM KGFDMEMENQ RKQSQAAHNV
VKLSVGNETE IVKNRTPFYA ESGGQVGDNG FLYVYGEEDA KQKAVIEIND VQKSLGNIFV
HKGTIKQGSV EVGREIDAAV DAKMRQGAKA HHTATHLLQS ALKNVIGSET SQAGSLVAFD
RLRFDFNFHR PLSEEELMKI ESLVNQWVSS ATHLETKVMD LQDAKNAGAI AMFGEKYGEQ
VRVVEVPGVS MELCGGTHVS NTAEIRGFKI ISEQGIASGV RRIEAVAGDA FVEYVCARDN
YMRRLCSSLK VKAEDVNGRV ETILEELRTT RNEVSSLRSK IAVLKAASLA SKATNIDNVR
VVVENMGEVD ADGLKSAAEY LVETLEDPAA VILGSSPGDG KVSLVAAFSP GVVKMRIQAG
KFVGGIAKLC GGGGGGKPNF AQAGGRKPEN LPGALEKARD EIVAAISSKS S
//
