ID A0A0E0PVQ6_ORYRU Unreviewed; 922 AA.
AC A0A0E0PVQ6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI06G09460.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI06G09460.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; A0A0E0PVQ6; -.
DR EnsemblPlants; ORUFI06G09460.1; ORUFI06G09460.1; ORUFI06G09460.
DR Gramene; ORUFI06G09460.1; ORUFI06G09460.1; ORUFI06G09460.
DR HOGENOM; CLU_004485_1_1_1; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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:UP000008022};
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 67..748
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 764..798
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
SQ SEQUENCE 922 AA; 100695 MW; 1655751C1A20E444 CRC64;
MEAAALLSPT ATSRSPLPLL STAPAAHRLH VLLPLSGRRR RLCLRSSPRP RVESATQEVG
AASSGEWSGD AIRRRFLDFY AARGHKILPS SSLVPDDPTV FLTIAGMLQF KPIFLGKEPR
RVPCATTSQK CIRTNDIENV GRTSRHQTFF EMLGNFSFGD YFKKEAITWA WELTTKEFGL
PPERLWISVF QDDDEAFSIW HNEVGVPKER IKRLGEDDNF WTSGATGPCG PCSEIYYDFY
PERGSSDADL GDDSRFIEFY NLVFMQYNKK DDGSLEPLKQ KNIDTGMGLE RMARILQKVP
NNYETDLIFP IIEKAASMAL VSYTTADDAM KTNLKIIGDH MRAVVYLISD GVIPSNIGRG
YVVRRLIRRV VRTGRLIGIR GDGHGNSEGA FLPSLAEVAI SLSTEIDPDV ESRRKSILGE
LQREELRFVQ TLERGEKLLD ELLDEALSSA GNNGGKPCLS GKDVFLLYDT YGFPVEITAE
IAGERGVIVD MKGFDMEMEN QRKQSQAAHN VVKLSVGNET EIVKNRTPFY AESGGQVGDN
GFLYVYGEED AKQKAVIEIN DVQKSLGNIF VHKGTIKQGS VEVGKEIDAA VDAKLRQGAK
AHHTATHLLQ SALKSIIGSE TSQAGSLVAF DRLRFDFNFH RPLSEEELMK IESLVNQWVS
SATHLETKVM DLQDAKNAGA IAMFGEKYGE QVRVVEVPGV SMELCGGTHV SNTAEIRGFK
IISEQGIASG VRRIEAVAGD AFVEYVCARD NYMRCLCSSL KVKAEDVNGR VETILEELRT
TRNEVSSLRS KIAVLKAASL ANKATTIDNT RVVVENMGDV DADGLKSAAE YLVDTLEDPA
AVILGSSPGD GKVSLVAAFS PGVVKMGIQA GKFVGGIAKL CGGGGGGKPN FAQAGGRKPE
NLPGALEKAR DEIVAAISSK SS
//
