ID A0A1U8DCA5_ALLSI Unreviewed; 1593 AA.
AC A0A1U8DCA5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Bifunctional glutamate/proline--tRNA ligase isoform X3 {ECO:0000313|RefSeq:XP_014374810.1};
GN Name=EPRS {ECO:0000313|RefSeq:XP_014374810.1};
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_014374810.1};
RN [1] {ECO:0000313|RefSeq:XP_014374810.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014374810.1; XM_014519324.2.
DR GeneID; 102381974; -.
DR CTD; 2058; -.
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; 4.
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; 4.
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; 4.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 4.
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; 4.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 4.
DR PROSITE; PS51185; WHEP_TRS_2; 4.
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_014374810.1};
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 980..1036
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1137..1377
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..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1092
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 960..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1593 AA; 179746 MW; EEF41F97B522A382 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 KSEKASKDKV DEAVRLLLSL KAEYKEKTGQ DYKPGHPPAA
QTSASPQATS IETSGSDTPE AKALYDKVAL QGEVVRKLKA EKAEKDKIDA AVQELLQLKA
QYKSFAGVDY KPASMTGIED KDKKKKEKEN KSEKQNKQQK QNETPKKESP KEQCANDLSS
NGAGEGQGPK KQTRLGLEAK KEENLADWFS QVITKSEMIE YYDVSGCYVL RPWAYAIWEA
IRDFFDTEIK KLGVENCYFP MFVSQAALEK EKTHIADFAP EVAWVTRSGK TELAEPIAVR
PTSETVMYPA YAKWVQSHRD LPIKLNQWCN VVRWEFKHPQ PFLRTREFLW QEGHTAFATY
EEAAEEVLQI LDLYARVYEE FLAIPVVKGR KTEKEKFAGG DYTTTVEAYI SASGRAIQGA
TSHHLGQNFS KMFEIVFEDP KKPGEKQLAY QNSWGITTRT IGVMTMIHGD NMGLVLPPRV
ACVQVIIIPC GITNSLSEED KDALLKKCND YLKRLLSVNI RVRADLRDNY SPGWKFNHWE
LKGVPIRLEV GPRDMKNHQF VAVRRDTGQK LTFAEDETED KLSQILEEIH ANLYNRAFED
LKNHMVVSND MDDFQKELDS GKIVQIPFCG EIECEDWIKK TTARDQDLEP GAPSMGAKSL
CIPFKPLCEL QAGTKCVCGK NPAKFYTLFG RSY
//
