ID A0A3S3Q1K7_9MAGN Unreviewed; 1004 AA.
AC A0A3S3Q1K7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN ORFNames=CKAN_00604400 {ECO:0000313|EMBL:RWR77553.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR77553.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR77553.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR77553.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR77553.1}.
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DR EMBL; QPKB01000002; RWR77553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3Q1K7; -.
DR STRING; 337451.A0A3S3Q1K7; -.
DR Proteomes; UP000283530; 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; 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; 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:UP000283530};
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 105..828
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 837..871
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
FT BINDING 789
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03134"
SQ SEQUENCE 1004 AA; 110569 MW; A26EA8E645E18BEE CRC64;
MEVSLLHPKA PHVRKPLFLV TASAASSSRS GVRKSNLLLT DASPGCKEHM SMIRTSIQVC
PRYSYYRHYH AAASKKVLFS IQNTSVSIQH ETKESVESTS KGHPVSGDGI RRRFLEFYAS
RGHKVLPSAS LVPDDPTVLL TIAGMLQFKP IFLGKAPRKV TRATTSQRCI RTNDVDNVGR
TTRHQTFFEM LGNFSFGDYF KREAINWAWD LTTKEFGLPP ERLWISVFED DDESFSIWRD
EVGVPVQQIK RMGEDDNFWT SGVTGPCGPC SEIYYDFHPE WGHSDVDLGD DARFIEFYNL
VFMQYNKKDD GSLEPLKDKN IDTGLGLERM ARILQKVPNN YETDLIYPII EKASELAGIS
YTDADDRLKT NLKIIGDHMR AVVYLISDGV FPSNIGRGYV VRRLIRRAVR TGRLLGIKGD
GKGNLEGAFL PTIAETVIEL STHIDSEVKA RTARILEELK REELRFVLTL ERGEKLLEQL
LTDALLTAQE NGSKPCLSGK DAFLLYDTYG FPVEITIEVA EERGVSVDMK DFDIQMENQK
RQSQAAHNVI KLSVGSASEL TECVSDTEFL GYDTLSARAV VEGLLVNGNP VIHVSEGSDV
EILLNKTPFY AESGGQIGDH GFLYVLGSEE TEHKAVVEIK DVRKSLGNIF VHKGTIKEGT
VEVGTEVDAA VDANLRQRAK VHHTATHLLQ AALKSVIGQE TSQAGSLVAF DRLRFDFNFH
RPLSEHELTE VEGSINRWIG NATYLQTKVM ALTDAKRAGA IAMFGEKYGE QVRVVEVPGV
SMELCGGTHV SNTAEIRAFK IISEQGIASG IRRIEAVAGD AFLDYINARD NHMRRLCSTL
KVKAEEVTAR VENLLEELRI MRNEVSVLRS QAATNKASAI ISKAISIGTS NIRVLVESMD
DMDSDSLKSA AEYVVDSLQD PAAVVLGSCP GEGKVSLAAS FTPGIVDLGI EAGKFIGPIA
KICGGGGGGR PNFAQAGGRK PENLLNALEK ARTDLIATLS EKAS
//
