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Database: UniProt
Entry: H2Q156_PANTR
LinkDB: H2Q156_PANTR
Original site: H2Q156_PANTR 
ID   H2Q156_PANTR            Unreviewed;      1512 AA.
AC   H2Q156; A0A2J8QV46;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Glutamyl-prolyl-tRNA synthetase {ECO:0000313|EMBL:JAA11206.1, ECO:0000313|Ensembl:ENSPTRP00000003343.4};
GN   Name=EPRS1 {ECO:0000313|Ensembl:ENSPTRP00000003343.4,
GN   ECO:0000313|VGNC:VGNC:1235};
GN   Synonyms=EPRS {ECO:0000313|EMBL:JAA11206.1};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000003343.4, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000003343.4, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA11206.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA11206.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA40271.1}, and Smooth vascular
RC   {ECO:0000313|EMBL:JAA17965.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000003343.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AACZ04071479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01000132; JAA11206.1; -; mRNA.
DR   EMBL; GABF01004180; JAA17965.1; -; mRNA.
DR   EMBL; GABE01004468; JAA40271.1; -; mRNA.
DR   RefSeq; XP_001172425.1; XM_001172425.4.
DR   PaxDb; 9598-ENSPTRP00000003343; -.
DR   Ensembl; ENSPTRT00000003628.5; ENSPTRP00000003343.4; ENSPTRG00000001995.5.
DR   GeneID; 457746; -.
DR   KEGG; ptr:457746; -.
DR   CTD; 2058; -.
DR   VGNC; VGNC:1235; EPRS1.
DR   eggNOG; KOG1147; Eukaryota.
DR   eggNOG; KOG4163; Eukaryota.
DR   GeneTree; ENSGT00550000074815; -.
DR   HOGENOM; CLU_001882_0_2_1; -.
DR   OMA; WDPKGNN; -.
DR   OrthoDB; 2733051at2759; -.
DR   TreeFam; TF300380; -.
DR   Proteomes; UP000002277; Chromosome 1.
DR   Bgee; ENSPTRG00000001995; Expressed in fibroblast and 21 other cell types or tissues.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00807; GlnRS_core; 1.
DR   CDD; cd10309; GST_C_GluProRS_N; 1.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   CDD; cd00936; WEPRS_RNA; 3.
DR   Gene3D; 1.20.1050.130; -; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 3.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   NCBIfam; TIGR00408; proS_fam_I; 1.
DR   PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF00458; WHEP-TRS; 3.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SMART; SM00991; WHEP-TRS; 3.
DR   SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 3.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 3.
DR   PROSITE; PS51185; WHEP_TRS_2; 3.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:JAA11206.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT   DOMAIN          749..805
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          822..878
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          900..956
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          1056..1296
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          709..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..729
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..987
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1006
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1512 AA;  170628 MW;  080E6540F6CB78E2 CRC64;
     MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR
     VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSAIN ELNHCLSLRT YLVGNSLSLA
     DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK
     KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
     PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
     AEREQRIESK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
     IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
     WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
     SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG
     LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
     YKKTTKITWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC
     LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI YIPDGHTKEM PTSGSKEKTK
     VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA
     VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL
     KAEKAPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
     AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED
     KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK
     EENLADWYSQ VITKSEMIEY HDVSGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM
     FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
     PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
     LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK
     IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK
     EALIAKCNDY RRRLLRVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV
     AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG
     KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
     PAKYYTLFGR SY
//
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