ID A0A3Q3L771_9TELE Unreviewed; 1496 AA.
AC A0A3Q3L771;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamyl-prolyl-tRNA synthetase 1 {ECO:0000313|Ensembl:ENSMAMP00000009242.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000009242.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000009242.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSMAMT00000009487.2; ENSMAMP00000009242.2; ENSMAMG00000006099.2.
DR GeneTree; ENSGT00550000074815; -.
DR Proteomes; UP000261640; Unplaced.
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; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
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; PF00043; GST_C; 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; PS50405; GST_CTER; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 3.
DR PROSITE; PS51185; WHEP_TRS_2; 3.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW 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:UP000261640}.
FT DOMAIN 36..171
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 732..788
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 804..860
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 881..937
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1029..1280
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 695..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1496 AA; 167307 MW; 6D1555B2643C6A5E CRC64;
MCSRIQSMTC LALLAAEHVK GSVQVSVAEG KETQFHVSEY IQFNDASSIS RYLARMAPAL
GLYGANIMEQ TEVDHWLEFS AQRLCCQPDL AVALGELDKV LSLRTYLVGH AITLADLSVW
AALKSNKEWP SLGKSFSHVN RWFSFLSSQV PFIAVGNKYA SNKLKEKKQD VGKFAELPGA
EMGKVVVRFP PEASGYLHIG HAKAALLNQH YQVTFKGKLI MRFDDTNPEK EKEDFEKVIL
EDVAMLQIHP DQFTYTSDHF AIILRFAEQL LVEGKAYIDD TPPEQMKQER EQRIESKCRN
NTVEQNMKMW SEMKAGTEHG QSCCMRAKID MNSNNGCLRD PTLYRCKNTP HPRTGTTYKV
YPTYDFACPI VDSLEGVTHA LRTTEYHDRD EQFYWVIDAL RLRKPYIWEY ARLNLNNTVL
SKRKLTWFVD QGYVDGWDDP RFPTVRGVLR RGMTVEGLKQ FIAAQGGSRS VVNMEWDKIW
AFNKKVIDPV APRYTALSSS YVVPVSIPEA KEEMKEVAKH PKNIDVGMKE VWYGPRVLID
GADAETFSEG ETVTFINWGN LIITKINKGP DGKVVSMEAR LNLDNKDFKK TTKITWLADT
NSAPLMPTVC ITYQPLISKA VIAKDDDFKE YINKDSKLEE KMLGDPCLKN LKKGDIIQLQ
RRGFYICDQP YEPISPNSCK ESPCVLLYIP DGHTKEMPTS GSKDKSKSQS SNNRASPTKA
ASTSAPVPAS TSASDLFSSI VSQGEAVRQL KTAKAPKDEI DVAVKQLLAL KAEFKKLTGQ
EYKPGMAPPT PTSTAPPSTP DSSSSSCLYA RVAQQGEVVR KLKSEKAPKD QVDAAVKQLL
ALKAEYKQQT GQDYKPGTQP PANAAQTESS SSSTTTSSSP QAQELFSQVS QQGELVRKLK
SEKAPKDQVD EAVKTLLDLK SRYKTLTGVE YKPVGAAGAT GGDDKNRKER ENKSEKQTGG
GAGAGKKSKG DKTSQGKESS GGAGGSGEGQ GPKKQTRLGL EAKKEENLAD WYSQVITKSE
MIEYYDVSGC YVLRPWAFAI WESIKEFFDR EIKKLGVENC YFPMFVSQAA LEKEKTHIAD
FAPEVAWVTR SGKTELAEPI AVRPTSETVM YPAYAKWVQS HRDLPIKLNQ WCNVVRWEFK
HPQPFLRTRE FLWQEGHTAF ATKEEAAEEV LQILDLYARV YEELMAIPVV KGRKTEKEKF
AGGDYTTTVE AFISASGRAI QGATSHHLGQ NFSRMFEIMF EDPKRPGEKQ LAFQNSWGIT
TRTIGVLTMV HGDNMGLVLP PRVACLQVIV IPCGITASLP EKEKEELLAQ CSKYMNRLQG
AGIRVKNDLR DNYSPGWKFN HWELKGVPVR LEVGPKDMQQ RQCVAVRRDS GAKVTIPEAD
VEEKLVAMLE DIQNSLYKKA SDDLKNHMVA VDTMEQFQKE LDQGKIVQIP FCGGIECEDW
IKKITAKDQD LEPGAPSMGA KSLCIPFSPL KTLQPGQMCV SGKELAQYYT MFGRSY
//
