SYHC_ARATH
ID SYHC_ARATH Reviewed; 883 AA.
AC F4IYF8; Q0WN73; Q9M8R8;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Histidine--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.21 {ECO:0000305};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000305};
DE Short=HisRS {ECO:0000305};
GN OrderedLocusNames=At3g02760 {ECO:0000312|Araport:AT3G02760};
GN ORFNames=F13E7.30;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 689-883.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
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 [5]
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).
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: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018363; AAF26984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73857.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63728.1; -; Genomic_DNA.
DR EMBL; AK229577; BAF01427.1; -; mRNA.
DR RefSeq; NP_001325800.1; NM_001337433.1.
DR RefSeq; NP_186925.4; NM_111144.6.
DR AlphaFoldDB; F4IYF8; -.
DR SMR; F4IYF8; -.
DR STRING; 3702.AT3G02760.1; -.
DR PaxDb; F4IYF8; -.
DR PRIDE; F4IYF8; -.
DR ProteomicsDB; 233059; -.
DR EnsemblPlants; AT3G02760.1; AT3G02760.1; AT3G02760.
DR EnsemblPlants; AT3G02760.2; AT3G02760.2; AT3G02760.
DR GeneID; 820930; -.
DR Gramene; AT3G02760.1; AT3G02760.1; AT3G02760.
DR Gramene; AT3G02760.2; AT3G02760.2; AT3G02760.
DR KEGG; ath:AT3G02760; -.
DR Araport; AT3G02760; -.
DR TAIR; locus:2075472; AT3G02760.
DR eggNOG; KOG1936; Eukaryota.
DR HOGENOM; CLU_006858_0_0_1; -.
DR InParanoid; F4IYF8; -.
DR OMA; ITGVFKM; -.
DR OrthoDB; 1065556at2759; -.
DR PRO; PR:F4IYF8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IYF8; baseline and differential.
DR Genevisible; F4IYF8; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 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; IPR033656; HisRS_anticodon.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..883
FT /note="Histidine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000433545"
SQ SEQUENCE 883 AA; 97537 MW; FD4819A500809171 CRC64;
MAAERSSITL GGKGSSLSSS SVYNVASGVA NVRIDSSAIE RFSTRNVPSI KRSSFGIPQG
LTNEETRASL AVLLNKLILS TSGPPSSSTA RSVLPLKIVE ILNLKAESLE LGEIDVTEGE
NIVLEKSCAS LIGICSIIDH KSTTLSQIVD SVAALSCEVT KADIASFSLL DSGDGNGDKD
VIGVAGDLKV LLNGYKGTGK LEIEEISKIP WIHGKFRYVV KSVHADARRE LNSGVKGGKT
GSGNTGIGEA LGTTLLPLLT AIKNLGVCSF LRAKLCFEKI VDENLKKCLS EKICVENENL
KNSYKLAYTA HLEEDYCRFA HKLNECLGIV WRIVGLEAVA AFFALAGGEL FVQKSGDADK
EESKTDKKKK KNEKKAVVGK GTSLVIQFIK DRLVSNDAAS DGDQMHSLMQ CGEQILNLFN
PEGRSFDSLL DKVKEIVESN ENRRLPKLPK GTRDFAKEQM AVREKAFSII QNVFKRHGAT
ALDTPVFELR ETLMGKYGED SKLVYDIADQ GGELCSLRYD LTVPFARYVA MNGITSFKRY
QIAKVYRRDN PSKGRYREFY QCDFDIAGLF EPMGPDFEIV KILTELLDEL EIGDYEVKLN
HRKLLDGMLE ICGVPPEKFR TICSSIDKLD KQSFEQVKKE MVEEKGLSSE IADRIGNFVK
EKGAPLELLS KLRQEGSEFL DNQSSREALD ELSIMFEALK RSKCSERIVF DLSLARGLDY
YTGVIFEAVC IGAEVGSIGA GGRYDNLIGM FGTKQVPAVG MSLGIERVFN IMEELNEKQK
QVIRPTETQV LVSIMVDNKL AEAAELVSQL WGAKINAEYL VSKRKEKHFN RAKESGIPWM
VMVGEKELSG SFVTLKKLEK GSEEKEDQTC TRDRFVEELK KLL
