SYAP_POPTR
ID SYAP_POPTR Reviewed; 994 AA.
AC B9HQZ6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Flags: Precursor;
GN ORFNames=POPTRDRAFT_821063;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nisqually;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S.,
RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S.,
RA Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M.,
RA Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B.,
RA Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D.,
RA Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J.,
RA Tuskan G., Rokhsar D.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000255|HAMAP-
CC Rule:MF_03134}. Mitochondrion {ECO:0000255|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:0000255|HAMAP-Rule:MF_03134}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03134}.
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DR EMBL; CM009298; EEE87638.1; -; Genomic_DNA.
DR RefSeq; XP_002313683.1; XM_002313647.2.
DR AlphaFoldDB; B9HQZ6; -.
DR SMR; B9HQZ6; -.
DR STRING; 3694.POPTR_0009s14340.1; -.
DR EnsemblPlants; PNT21320; PNT21320; POPTR_009G141300v3.
DR GeneID; 7472090; -.
DR Gramene; PNT21320; PNT21320; POPTR_009G141300v3.
DR KEGG; pop:7472090; -.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_1_1_1; -.
DR InParanoid; B9HQZ6; -.
DR Proteomes; UP000006729; Chromosome 9.
DR ExpressionAtlas; B9HQZ6; baseline and differential.
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; 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: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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT CHAIN ?..994
FT /note="Alanine--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000402310"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 774
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
SQ SEQUENCE 994 AA; 109537 MW; 266989378EFB2021 CRC64;
MGGLKLPPQT LHGIHGGRRP LTAPSSKPSF TIQPNYSSSI STGFTTRNVA LFSPSIFPCG
YFILGGARER RFGARNTQAS VQPVTEELVE DKTKENPVSG DAIRRRFLEF YASRSHKVLP
SASLVPDDPT VLLTIAGMLQ FKPIFLGKAP RQVPRATTAQ KCIRTNDVEN VGRTTRHHTF
FEMLGNFSFG DYFKKEAIKW AWELSTKEFG LPADRLWVSV YEDDDEAFEI WHDEVGVPVE
RIKRMGEEDN FWTSGATGPC GPCSELYYDF HPERGYKNTD LGDDSRFIEF YNLVFMQYNK
MDDGSLEPLK QKNIDTGLGL ERLARILQKV PNNYETDLIY PIIEKAAELA NISYALADDR
TKMNLKIIGD HLRAIVYLIS DGVLPSNIGR GYVVRRLIRR AVRTGRLLGV KGGGEDGVFL
PAIAEKVIEL SPHIDPDVKA RGHSILDELQ REELRFVQTL ERGEKLLDQM LAEALLNAQK
SETLPCLSGK DVFLLYDTFG FPVEITTEVA EEQGVKIDMD GFEVEMENQR RQSQAAHNVV
KLAVENGGDL AENVHDTEFL GYDTLSARAV VESLLLNGKS VIQVSEGSEV EVLLNKTPFY
AESGGQIGDH GFLYVTQDQS KQTAVVEIKD VQKSLGSVFV HKGTIREGVL EVGREVEAAV
DAKLRQRAKV HHTATHLLQS ALKKVIGQET SQAGSLVAFD RLRFDFNFHR PLHDSELEEI
ENLINGWIGD GTLLQTKVMS LTDAKEAGAI AMFGEKYGEQ VRVVEVPGVS MELCGGTHVS
NTSEIRAFKI ISEQGIASGI RRIEAVAGEA FIEYINARDS QMKLLCSTLK VKAEEVTTRV
DNLLEELRTV RNEVSALRAK AAVYKASMIA SKAFSVGTSK TIRVLVESMD DFDADALKSA
AEYLMDTLQD PAAIILGSCP DEGKVSLVAA FTPGVVDIGI QAGKFIGPIA KLCGGGGGGR
PNFAQAGGRK PENLTNALEK ARTDLILILT EKAN
