ID A0A1U8DAR2_ALLSI Unreviewed; 1676 AA.
AC A0A1U8DAR2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Bifunctional glutamate/proline--tRNA ligase isoform X1 {ECO:0000313|RefSeq:XP_014374809.1};
GN Name=EPRS {ECO:0000313|RefSeq:XP_014374809.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014374809.1};
RN [1] {ECO:0000313|RefSeq:XP_014374809.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014374809.1; XM_014519323.2.
DR STRING; 38654.A0A1U8DAR2; -.
DR GeneID; 102381974; -.
DR CTD; 2058; -.
DR InParanoid; A0A1U8DAR2; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000189705; 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; 5.
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; 5.
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; 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; 5.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 5.
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; 5.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 5.
DR PROSITE; PS51185; WHEP_TRS_2; 5.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_014374809.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 749..805
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 825..881
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 902..958
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 985..1041
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1063..1119
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1220..1460
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 707..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 709..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1676 AA; 188633 MW; A221F496D851C719 CRC64;
MALSLTVNVG NPPLGALLTV EHVKNDFEIL VEEGKETVLR ISDHVTFTDA NSIARYLARV
ATSAGLYGSN LLEHTEIDHW LEFSATKLSA PSQFPSAIHE LNHCLSLRTY LVGNSLSLAD
LCVWAVLKGS NIWQEELQQN KAPVHVKRWY DFLEAQCAFQ SVGTKWAAAT PKTNVATEKK
QDVGKFVELP GAEVGKVIVR FPPEASGYLH IGHAKAALLN QHYQVNFKGK LIMRFDDTNP
EKEKEDFEKV ILEDVAMLHI KPDQFTYTSD HFETIMKYAE KLIQEGKAYV DNTPAEQMKM
EREQRKESKH RNNSVEKNLE MWEEMKKGTE YGQTCCLRAK IDMSCNNGCM RDPTLYRCKN
QPHPRTGNTY KVYPTYDFAC PIVDSIEGVT HALRTTEYHD RDEQFYWIIE ALGIRKPYIW
EYSRLNLNNT VLSKRKLTWF VNEGLVDGWD DPRFPTVRGV LRRGMTVEGL KQFIAAQGSS
RSVVNMEWDK IWAFNKKVID PVAPRYTALL KDDVVTVNIP EAVEEMKEVA KHPKNPDVGL
KPVWYGSRVL IEGADADTLT EGEMVTFINW GNIIITKIHR NSNRKIVSID AKLNLENKDY
KKTAKITWLT NTPSAPLIPS VCVNYEHLIT KPVLGKDEDF KQYVNRNSKQ EELMLGDPCL
KELKKGDIIQ LQRRGFFICD QPYEPISPYS CKEAPCILIY IPDGHTKEMP TSGSKEKTKA
ETAKKEASSA SKEKPTPPFV ADTSTAPADP VVLYNRVSAQ GDVVRDLKAK KASKEDIDAA
VKQLLALKAE YREKTGQEYK PGSHPAAAAS VPSVPSNLET SSMLDSTTLY DKVAEQGDMV
RKLKAERAPK DQIDAAVKVL LTLKSEYKQQ TGQEYKPGNP PATVIPSKSS PVSTSTSPCP
TDSKSLYSKV AEQGEVVRRL KSEKASKEQI DDAVKVLLTL KAEYKQKTGQ EYKPGNPPAS
SLCTSSSASF LSTSCNNLTS SSSVDSKMLY DKVAEQGEVV RSLKAEKASK DKVDEAVRLL
LSLKAEYKEK TGQDYKPGHP PAAQTSASPQ ATSIETSGSD TPEAKALYDK VALQGEVVRK
LKAEKAEKDK IDAAVQELLQ LKAQYKSFAG VDYKPASMTG IEDKDKKKKE KENKSEKQNK
QQKQNETPKK ESPKEQCAND LSSNGAGEGQ GPKKQTRLGL EAKKEENLAD WFSQVITKSE
MIEYYDVSGC YVLRPWAYAI WEAIRDFFDT EIKKLGVENC YFPMFVSQAA LEKEKTHIAD
FAPEVAWVTR SGKTELAEPI AVRPTSETVM YPAYAKWVQS HRDLPIKLNQ WCNVVRWEFK
HPQPFLRTRE FLWQEGHTAF ATYEEAAEEV LQILDLYARV YEEFLAIPVV KGRKTEKEKF
AGGDYTTTVE AYISASGRAI QGATSHHLGQ NFSKMFEIVF EDPKKPGEKQ LAYQNSWGIT
TRTIGVMTMI HGDNMGLVLP PRVACVQVII IPCGITNSLS EEDKDALLKK CNDYLKRLLS
VNIRVRADLR DNYSPGWKFN HWELKGVPIR LEVGPRDMKN HQFVAVRRDT GQKLTFAEDE
TEDKLSQILE EIHANLYNRA FEDLKNHMVV SNDMDDFQKE LDSGKIVQIP FCGEIECEDW
IKKTTARDQD LEPGAPSMGA KSLCIPFKPL CELQAGTKCV CGKNPAKFYT LFGRSY
//
