位置:首页 > 蛋白库 > SYAP_ARATH
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};
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024