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Entry version 77 (26 Feb 2020)
Sequence version 3 (23 May 2018)
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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS1 function from protein synthesis to translation inhibition. Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei211ATPBy similarity1
Binding sitei398ATPBy similarity1
Binding sitei1151L-prolineBy similarity1
Binding sitei1241L-prolineBy similarity1
Binding sitei1275ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1447ZincBy similarity1
Metal bindingi1452ZincBy similarity1
Metal bindingi1494ZincBy similarity1
Metal bindingi1496ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi432 – 436ATPBy similarity5
Nucleotide bindingi1151 – 1153ATPBy similarity3
Nucleotide bindingi1162 – 1163ATPBy similarity2
Nucleotide bindingi1236 – 1239ATPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, Multifunctional enzyme, RNA-binding
Biological processProtein biosynthesis, Translation regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase
Including the following 2 domains:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Proline--tRNA ligase (EC:6.1.1.15By similarity)
Alternative name(s):
Prolyl-tRNA synthetase
Short name:
ProRS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EPRS1
Synonyms:EPRS, QPRS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10029 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197421 – 1511Bifunctional glutamate/proline--tRNA ligaseAdd BLAST1511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei300N6-acetyllysine; alternateBy similarity1
Modified residuei300N6-malonyllysine; alternateBy similarity1
Modified residuei355PhosphothreonineBy similarity1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei498N6-acetyllysineBy similarity1
Modified residuei535N6-acetyllysineBy similarity1
Modified residuei542N6-acetyllysineBy similarity1
Modified residuei637N6-acetyllysineBy similarity1
Modified residuei746PhosphoserineBy similarity1
Modified residuei787N6-acetyllysineBy similarity1
Modified residuei860N6-acetyllysineBy similarity1
Modified residuei871PhosphotyrosineBy similarity1
Modified residuei885Phosphoserine; by CDK5By similarity1
Modified residuei897PhosphothreonineBy similarity1
Modified residuei997PhosphoserineBy similarity1
Modified residuei998Phosphoserine; by RPS6KB1By similarity1
Modified residuei999PhosphoserineBy similarity1
Modified residuei1151Omega-N-methylarginineBy similarity1
Modified residuei1349PhosphoserineBy similarity1
Modified residuei1502N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Ser-998 by RPS6KB1; triggers EPRS1 release from the aminoacyl-tRNA synthetase multienzyme complex. In monocytes, the IFN-gamma-induced phosphorylation at Ser-998 releases EPRS1 from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex. Phosphorylation at Ser-998 is specifically required for the RPL13A-mediated interaction of the GAIT complex with eIF4G. Phosphorylation at Ser-998 by RPS6KB1, is also induced by insulin through activation of the mTORC1 signaling pathway and promotes the interaction of EPRS1 with SLC27A1.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q7SIA2

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that is composed of the tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18.

Forms a linear complex that contains MARS1, EEF1E1, EPRS1 and AIMP2 that is at the core of the multisubunit complex.

Interacts with TARS3.

Interacts with DUS2L.

Component of the GAIT complex which is composed of EPRS1, RPL13A and GAPDH.

Interacts (phosphorylated at Ser-998) with SLC27A1; mediates the translocation of SLC27A1 from the cytoplasm to the plasma membrane thereby increasing the uptake of long-chain fatty acids.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10029.XP_007636777.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q7SIA2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q7SIA2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini748 – 804WHEP-TRS 1PROSITE-ProRule annotationAdd BLAST57
Domaini821 – 877WHEP-TRS 2PROSITE-ProRule annotationAdd BLAST57
Domaini899 – 955WHEP-TRS 3PROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni164 – 758Glutamate--tRNA ligaseBy similarityAdd BLAST595
Regioni759 – 9553 X 57 AA approximate repeatsBy similarityAdd BLAST197
Regioni958 – 990ChargedBy similarityAdd BLAST33
Regioni1006 – 1511Proline--tRNA ligaseBy similarityAdd BLAST506
Regioni1120 – 1122L-proline bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi204 – 214'HIGH' regionAdd BLAST11
Motifi432 – 436'KMSKS' region5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi960 – 990Lys-richPROSITE-ProRule annotationAdd BLAST31

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The WHEP-TRS domains are involved in RNA binding.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00778 ProRS_core_arch_euk, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.240.10, 2 hits
3.30.110.30, 1 hit
3.40.50.620, 1 hit
3.40.50.800, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02076 Glu_tRNA_synth_type2, 1 hit
MF_01571 Pro_tRNA_synth_type3, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR001412 aa-tRNA-synth_I_CS
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR004046 GST_C
IPR004499 Pro-tRNA-ligase_IIa_arc-type
IPR016061 Pro-tRNA_ligase_II_C
IPR017449 Pro-tRNA_synth_II
IPR033721 ProRS_core_arch_euk
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
IPR009068 S15_NS1_RNA-bd
IPR000738 WHEP-TRS_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00043 GST_C, 1 hit
PF03129 HGTP_anticodon, 1 hit
PF09180 ProRS-C_1, 1 hit
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF00458 WHEP-TRS, 3 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00987 TRNASYNTHGLU

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00946 ProRS-C_1, 1 hit
SM00991 WHEP-TRS, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47060 SSF47060, 3 hits
SSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit
SSF64586 SSF64586, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00463 gltX_arch, 1 hit
TIGR00408 proS_fam_I, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit
PS50862 AA_TRNA_LIGASE_II, 1 hit
PS00762 WHEP_TRS_1, 2 hits
PS51185 WHEP_TRS_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q7SIA2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAALCLTVNA GDPPLDALLA VEHVKGDVSV SVEEGKENLL RVSEDVVFTD
60 70 80 90 100
INSILRYLAR VATTSGLYGT NLMEHTEIDH WLEFSATKLS SCAALTSALT
110 120 130 140 150
ELNHCLSLRT YLVGNSLTLA DLCVWATLKG NAAWQEQLEQ NKTLVHVKRW
160 170 180 190 200
FGFLEAQQAF RSVGTKWDVS ENKARVVPDK KQDVGKFVEL PGAEMGKVTV
210 220 230 240 250
RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK
260 270 280 290 300
VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
310 320 330 340 350
AEREQRAESK HRQNSVEKNL QMWEEMKKGS PFGQSCCLRA KIDMSSNNGC
360 370 380 390 400
MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH
410 420 430 440 450
DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW
460 470 480 490 500
DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI
510 520 530 540 550
DPVAPRYVAL LKKEVVPVNV PEAQEEMKEV ARHPKNPDVG LKPVWYSPKV
560 570 580 590 600
FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD
610 620 630 640 650
YKKTTKITWL AETTHALPIP AICVTYEHLI TKPVLGKDED FKQYVNKDSK
660 670 680 690 700
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCILI
710 720 730 740 750
YIPDGHTKEM PTSGSKEKTK AEPLKKETSS APKEGPVPAV SPCAASEESS
760 770 780 790 800
VLYNRVAAQG DVVRELKAKK AAKEDVDAAV KQLLALKAEY KQKTGQEYKP
810 820 830 840 850
GNPPSAAAQS ASTKSLPSAG EDRSLYDKIA AQGEVVRKLK AEKAPKAKVT
860 870 880 890 900
EAVECLLSLK AEYKEKTGKE YVPGQPPASQ KSQPSPASKA EPAGPETTEA
910 920 930 940 950
KALFDRVACQ GEVVRKLKAE KASKDQVDPA VQELLQLKAQ YKSLTGIEYK
960 970 980 990 1000
PVSATGSEDK DKKKKEKENK SEKQNKPQKQ NDGPGKDSSK SQGGGLSSSG
1010 1020 1030 1040 1050
AGEGQGPKKQ TRLGLEAKKE ENLAEWYSQV ITKSEMIEYY DVSGCYILRP
1060 1070 1080 1090 1100
WSYSIWESIK DFFDTEIKKL GVENCYFPIF VSQAALEKEK SHIEDFAPEV
1110 1120 1130 1140 1150
AWVTRSGKTE LAEPIAIRPT SETVMYPAYA KWVQSHRDLP IRLNQWCNVV
1160 1170 1180 1190 1200
RWEFKHPQPF LRTREFLWQE GHSAFATFEE AADEVMQILE LYARVYEELL
1210 1220 1230 1240 1250
AIPVVRGRKT EKEKFAGGDY TTTVEAFISA SGRAIQGATS HHLGQNFSKM
1260 1270 1280 1290 1300
CEIVFEDPKT PGEKQFAFQC SWGLTTRTIG VMIMVHGDNM GLVLPPRVAC
1310 1320 1330 1340 1350
VQVVVIPCGI TNALSEEDRE ALMAKCNEYR KRLLGVNIRV RVDLRDNYSP
1360 1370 1380 1390 1400
GWKFNHWELK GVPVRLEVGP RDMKSCQFVA VRRDTGEKLT IAEKEAESKL
1410 1420 1430 1440 1450
QEILEDIQLN LFTRASEDLK THMVVSNTLE DFQKVLDSGK IAQIPFCGEI
1460 1470 1480 1490 1500
DCEDWIKKTT ARDQDVEPGA PSMGAKSLCI PFTPLCELQP GAMCVCGKNP
1510
AKFYTLFGRS Y
Length:1,511
Mass (Da):169,781
Last modified:May 23, 2018 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i58CC131EAD375785
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AMDS01047676 Genomic DNA No translation available.
AMDS01047677 Genomic DNA No translation available.
AMDS01047678 Genomic DNA No translation available.
AMDS01047679 Genomic DNA No translation available.
AMDS01047680 Genomic DNA No translation available.

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSCGRT00001011517; ENSCGRP00001007475; ENSCGRG00001009885

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AMDS01047676 Genomic DNA No translation available.
AMDS01047677 Genomic DNA No translation available.
AMDS01047678 Genomic DNA No translation available.
AMDS01047679 Genomic DNA No translation available.
AMDS01047680 Genomic DNA No translation available.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2DNMR-A826-874[»]
1R1BNMR-A826-874[»]
SMRiQ7SIA2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10029.XP_007636777.1

Proteomic databases

PRIDEiQ7SIA2

Genome annotation databases

EnsembliENSCGRT00001011517; ENSCGRP00001007475; ENSCGRG00001009885

Miscellaneous databases

EvolutionaryTraceiQ7SIA2

Family and domain databases

CDDicd00778 ProRS_core_arch_euk, 1 hit
Gene3Di2.40.240.10, 2 hits
3.30.110.30, 1 hit
3.40.50.620, 1 hit
3.40.50.800, 1 hit
HAMAPiMF_02076 Glu_tRNA_synth_type2, 1 hit
MF_01571 Pro_tRNA_synth_type3, 1 hit
InterProiView protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR001412 aa-tRNA-synth_I_CS
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR004046 GST_C
IPR004499 Pro-tRNA-ligase_IIa_arc-type
IPR016061 Pro-tRNA_ligase_II_C
IPR017449 Pro-tRNA_synth_II
IPR033721 ProRS_core_arch_euk
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
IPR009068 S15_NS1_RNA-bd
IPR000738 WHEP-TRS_dom
PfamiView protein in Pfam
PF00043 GST_C, 1 hit
PF03129 HGTP_anticodon, 1 hit
PF09180 ProRS-C_1, 1 hit
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF00458 WHEP-TRS, 3 hits
PRINTSiPR00987 TRNASYNTHGLU
SMARTiView protein in SMART
SM00946 ProRS-C_1, 1 hit
SM00991 WHEP-TRS, 3 hits
SUPFAMiSSF47060 SSF47060, 3 hits
SSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit
SSF64586 SSF64586, 1 hit
TIGRFAMsiTIGR00463 gltX_arch, 1 hit
TIGR00408 proS_fam_I, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit
PS50862 AA_TRNA_LIGASE_II, 1 hit
PS00762 WHEP_TRS_1, 2 hits
PS51185 WHEP_TRS_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYEP_CRIGR
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q7SIA2
Secondary accession number(s): Q7SIG9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 23, 2018
Last modified: February 26, 2020
This is version 77 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
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