SYHM_ARATH
ID SYHM_ARATH Reviewed; 486 AA.
AC O82413;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Histidine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.21 {ECO:0000305};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000305};
DE Short=HisRS {ECO:0000305};
DE AltName: Full=Histidyl-tRNA synthetase 1 {ECO:0000303|PubMed:9684861};
DE Short=AtHRS1 {ECO:0000303|PubMed:9684861};
DE Flags: Precursor;
GN OrderedLocusNames=At3g46100 {ECO:0000312|Araport:AT3G46100};
GN ORFNames=F12M12_70 {ECO:0000312|EMBL:CAB90937.1};
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=9684861; DOI=10.1016/s0014-5793(98)00717-0;
RA Akashi K., Grandjean O., Small I.;
RT "Potential dual targeting of an Arabidopsis archaebacterial-like histidyl-
RT tRNA synthetase to mitochondria and chloroplasts.";
RL FEBS Lett. 431:39-44(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9684861}. Mitochondrion
CC {ECO:0000269|PubMed:9684861}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AF020715; AAC61600.1; -; mRNA.
DR EMBL; AL355775; CAB90937.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78113.1; -; Genomic_DNA.
DR EMBL; AY056233; AAL07082.1; -; mRNA.
DR EMBL; AY117252; AAM51327.1; -; mRNA.
DR PIR; T49251; T49251.
DR RefSeq; NP_190196.1; NM_114479.5.
DR AlphaFoldDB; O82413; -.
DR SMR; O82413; -.
DR STRING; 3702.AT3G46100.1; -.
DR PaxDb; O82413; -.
DR PRIDE; O82413; -.
DR ProteomicsDB; 233041; -.
DR EnsemblPlants; AT3G46100.1; AT3G46100.1; AT3G46100.
DR GeneID; 823753; -.
DR Gramene; AT3G46100.1; AT3G46100.1; AT3G46100.
DR KEGG; ath:AT3G46100; -.
DR Araport; AT3G46100; -.
DR TAIR; locus:2075306; AT3G46100.
DR eggNOG; KOG1936; Eukaryota.
DR HOGENOM; CLU_025113_3_1_1; -.
DR InParanoid; O82413; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 1065556at2759; -.
DR PhylomeDB; O82413; -.
DR BRENDA; 6.1.1.21; 399.
DR PRO; PR:O82413; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82413; baseline and differential.
DR Genevisible; O82413; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; ISS:TAIR.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISS:TAIR.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..486
FT /note="Histidine--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433546"
SQ SEQUENCE 486 AA; 54559 MW; 9DFD426B209C111F CRC64;
MRAIHIVTTR LSSSFRPILL LDLVSSCSPP RQFSIPRRLI CAAANGGGRS GSIVAPLVTE
EDFHKKIDVN PPKGTRDFPP EDMRLRNWLF NHFKEVSRLY GYEEVDYPVL ETEALFIRKA
GEEIRDQLYC FEDRGNRRVA LRPELTPSLA RLVIQKGKSV SLPLKWFAIG QCWRYERMTR
GRRREHYQWN MDIIGVPQVT AEAELISSIV TFFKRIGITA SDVGFKVSSR KVLQELLKKY
GVPEDLFGRV CIIIDKIEKI PIDEIKKELG FTGISEDAIE QLLQVLSVKS LDDLEDIIGG
AGEAIADLKQ LFSLAEKFGY SEWIQFDASV VRGLAYYTGI VFEGFDRKGK LRAICGGGRY
DRLLSTYGGD DFPACGFGFG DAVIVELLKE KDLLPELGQE VENIVCALDK DLQGAAATVA
TALRDKGQTV DLVLESKPLK WVFKRAARVN ARRLVLVGKT EWEDGSVSVK VLSSGEQFQV
KLSDLE
