SYAP_ARATH
ID SYAP_ARATH Reviewed; 978 AA.
AC Q9FFC7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alanine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03134};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03134};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03134};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03134};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1030 {ECO:0000305|PubMed:16297076};
DE AltName: Full=Protein EMBRYO DEFECTIVE 263;
DE AltName: Full=Protein EMBRYO DEFECTIVE 86;
DE Flags: Precursor;
GN Name=EMB86; Synonyms=EMB1030 {ECO:0000305|PubMed:16297076}, EMB263;
GN OrderedLocusNames=At5g22800; ORFNames=MRN17.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-773, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
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_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:0000255|HAMAP-Rule:MF_03134};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03134};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03134};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03134}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_03134}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC embryo at early cotyledon stage. {ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03134}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005243; BAB10601.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93081.1; -; Genomic_DNA.
DR RefSeq; NP_680210.2; NM_147905.3.
DR AlphaFoldDB; Q9FFC7; -.
DR SMR; Q9FFC7; -.
DR BioGRID; 17618; 1.
DR STRING; 3702.AT5G22800.1; -.
DR iPTMnet; Q9FFC7; -.
DR MetOSite; Q9FFC7; -.
DR PaxDb; Q9FFC7; -.
DR PRIDE; Q9FFC7; -.
DR ProteomicsDB; 226791; -.
DR EnsemblPlants; AT5G22800.1; AT5G22800.1; AT5G22800.
DR GeneID; 832343; -.
DR Gramene; AT5G22800.1; AT5G22800.1; AT5G22800.
DR KEGG; ath:AT5G22800; -.
DR Araport; AT5G22800; -.
DR TAIR; locus:504954871; AT5G22800.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_1_1_1; -.
DR InParanoid; Q9FFC7; -.
DR OMA; DMEMENQ; -.
DR PhylomeDB; Q9FFC7; -.
DR PRO; PR:Q9FFC7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFC7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
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 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 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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Isopeptide bond;
KW Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide;
KW tRNA-binding; Ubl conjugation; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT CHAIN ?..978
FT /note="Alanine--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000402303"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 758
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 762
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT CROSSLNK 773
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 978 AA; 107830 MW; FB7DB42432F99CAC CRC64;
MNFSRVNLFD FPLRPILLSH PSSIFVSTRF VTRTSAGVSP SILLPRSTQS PQIIAKSSSV
SVQPVSEDAK EDYQSKDVSG DSIRRRFLEF FASRGHKVLP SSSLVPEDPT VLLTIAGMLQ
FKPIFLGKVP REVPCATTAQ RCIRTNDLEN VGKTARHHTF FEMLGNFSFG DYFKKEAIKW
AWELSTIEFG LPANRVWVSI YEDDDEAFEI WKNEVGVSVE RIKRMGEADN FWTSGPTGPC
GPCSELYYDF YPERGYDEDV DLGDDTRFIE FYNLVFMQYN KTEDGLLEPL KQKNIDTGLG
LERIAQILQK VPNNYETDLI YPIIAKISEL ANISYDSAND KAKTSLKVIA DHMRAVVYLI
SDGVSPSNIG RGYVVRRLIR RAVRKGKSLG INGDMNGNLK GAFLPAVAEK VIELSTYIDS
DVKLKASRII EEIRQEELHF KKTLERGEKL LDQKLNDALS IADKTKDTPY LDGKDAFLLY
DTFGFPVEIT AEVAEERGVS IDMNGFEVEM ENQRRQSQAA HNVVKLTVED DADMTKNIAD
TEFLGYDSLS ARAVVKSLLV NGKPVIRVSE GSEVEVLLDR TPFYAESGGQ IADHGFLYVS
SDGNQEKAVV EVSDVQKSLK IFVHKGTVKS GALEVGKEVE AAVDADLRQR AKVHHTATHL
LQSALKKVVG QETSQAGSLV AFDRLRFDFN FNRSLHDNEL EEIECLINRW IGDATRLETK
VLPLADAKRA GAIAMFGEKY DENEVRVVEV PGVSMELCGG THVGNTAEIR AFKIISEQGI
ASGIRRIEAV AGEAFIEYIN SRDSQMTRLC STLKVKAEDV TNRVENLLEE LRAARKEASD
LRSKAAVYKA SVISNKAFTV GTSQTIRVLV ESMDDTDADS LKSAAEHLIS TLEDPVAVVL
GSSPEKDKVS LVAAFSPGVV SLGVQAGKFI GPIAKLCGGG GGGKPNFAQA GGRKPENLPS
ALEKAREDLV ATLSEKLG
