ID A0A091RT32_MERNU Unreviewed; 1584 AA.
AC A0A091RT32;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000313|EMBL:KFQ31612.1};
DE Flags: Fragment;
GN ORFNames=N331_04776 {ECO:0000313|EMBL:KFQ31612.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ31612.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ31612.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ31612.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK708009; KFQ31612.1; -; Genomic_DNA.
DR Proteomes; UP000052967; Unassembled WGS sequence.
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; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KFQ31612.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967}.
FT DOMAIN 738..794
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 811..867
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 894..950
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 971..1027
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1128..1368
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 694..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ31612.1"
FT NON_TER 1584
FT /evidence="ECO:0000313|EMBL:KFQ31612.1"
SQ SEQUENCE 1584 AA; 177906 MW; D838FE27003D237E CRC64;
GALLTVEHVK NDVEISVEEG KETILRVSEH VSFTEVNSIA RYLARVAASA GLYGSNLLEH
TEIDHWLEFS VTKLSTAKQL LSAVQELNHC LSLRTYLVGN SLSLADLCVW AALRDNNVWQ
EQLQQNRAPV HAKRWYGFLE AQRAFQAVGA KWASGTPKVK MATEKKADVG KFVELPGAEM
GKVIVRFPPE ASGYLHIGHA KAALLNQHYQ VTFKGKLIMR FDDTNPEKEK EDFEKVILED
VAMLHIKPDQ FTYTSDHFET IMKYAEKLIQ EGKAYVDDTP AEQMKAEREQ RVESKHRNNC
VNKNLQMWEE MKKGTEYGQT CCLRAKIDMS SNNGCMRDPT LYRCKNQPHP RTGSTYKVYP
TYDFACPIVD SIEGVTHALR TTEYHDRDEQ FYWIIEALGI RKPYIWEYSR LNLNNTVLSK
RKLTWFVNEG LVDGWDDPRF PTVRGVLRRG MTVEGLKQFI AAQGSSRSVV NMEWDKIWSF
NKKVIDPVAP RYTALLKDAV VPVCIPEAQE EMKEVAKHPK NADVGLKPVW YGSRVLIEGA
DAETLTEGEV VTFINWGNII ISKLNRNSSG KIVSIDAKLN LENKDFKKTT KITWLAETPS
APLIPTVCVN YEHLITKPVL GKDEDFKQYI NQNSKQEELM LGDPCLRELK KGDIIQLQRR
GFFICDQPYE PVSPYSCKDA PCILIYIPDG HTKEMPTSGS KEKTKAETAK KEAGSATKGK
SAPVVGDTST PTCAPSEGHL VIYNRVSAQG DIVRDLKAKK AAKEDIDKAV KQLLALKAEY
KEKTGQEYKP GNPPVSVSKQ SSKLETSGTL DSKALYDKVA EQGEVVRKLK AEKAPKEQID
EAVKILLNLK AEYKQKTGQE YKPGNPPSAP PCIPSTTVPS SVCCSNLAPC SLVDGKALYD
NVAEQGEVVR RLKADKASKD EIDEAVKLLL SLKADYKEKT GQDYKPGNPP VAQGALPQAS
NTVPSGPDTP EAKALFSKVA LQGDEVRKLK AEKAEKEKID AAVKELLHLK AQYKSVAGVE
YKPVSASGTD DKDKKKKEKD NKSEKQSKQQ KQNDGPKKEP LQGQGGSELS SSGSGEGQGP
KKQTRLGLEA KKEENLADWF SQVITKSEMI EYYDVSGCYV LRPWAYAIWE AIKNFFDAEI
KKLGVENCYF PMFVSQAALE KEKTHIADFA PEVAWVTRSG KTDLAEPIAV RPTSETVMYP
AYAKWVQSHR DLPIKLNQWC NVVRWEFKHP QPFLRTREFL WQEGHTAFAT YEEAAEEVMQ
ILDLYAQVYE DLLAIPVVKG RKTEKEKFAG GDYTTTVEAF ISASGRAIQG ATSHHLGQNF
SKMFEIVFED PKKPGEKQFA YQNSWGITTR TIGVMTMIHG DNMGLVLPPR VACVQVVIIP
CGITNSLSEE DKEALLKKCN EYRNRLLSAA VRVRADLRDN YSPGWKFNHW ELKGVPVRVE
VGPRDMKSQQ FVAVRRDTGQ KLTFSEHEAE DRLKQILEEI HTNLYNRASE DLKSHMVVAN
TMEDFQKELD SGKIVQIPFC GEIECEDWIK KTTARDQDLE PGAPSMGAKS LCIPFQPLCE
LQRGARCVCG KNPAKFYTLF GRSY
//
