ID A0A091JXK0_COLST Unreviewed; 1583 AA.
AC A0A091JXK0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000313|EMBL:KFP28673.1};
DE Flags: Fragment;
GN ORFNames=N325_06587 {ECO:0000313|EMBL:KFP28673.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP28673.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP28673.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP28673.1};
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; KK533276; KFP28673.1; -; Genomic_DNA.
DR Proteomes; UP000053615; 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; 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:KFP28673.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053615}.
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 893..949
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 970..1026
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1127..1367
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 694..732
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 939..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1084
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 1025..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP28673.1"
FT NON_TER 1583
FT /evidence="ECO:0000313|EMBL:KFP28673.1"
SQ SEQUENCE 1583 AA; 178086 MW; 455827123F5F3175 CRC64;
GALLTVEHAK NDVDISVEEG KETILRVSEH VSFTDVNSIV RYLARAGASA GLYGSNLVEH
TEIDHWLEFS ATKLSTANQF LSAVEELNHC LSLRTYLVGN SLSLADLCVW AVLKDNSTWQ
EQIQQNKAPV HAKRWYSFLE VQPTFQSVGT KWASGTPKVK MAAEKKADVG KFVELPGAEM
GKVIVRFPPE ASGYLHIGHA KAALLNQHYQ VNFKGKLIMR FDDTNPEKEK EDFEKVILED
VAMLHIKPDQ FTYTSDHFET IMKYAEKLIQ EGKAYVDDTP AEQMKAEREQ RMESKHRNNC
VNKNLQMWEE MKKGTEYGQT CCLRAKIDMS SNNGCMRDPT LYRCKNQPHP RTGSTYKVYP
TYDFACPIVD SIEGVTHALR TTEYHDRDEQ FYWIIEALGI RKPYIWEYSR LNLNNTVLSK
RKLTWFVNEG LVDGWDDPRF PTVRGVLRRG MTVEGLKQFI AAQGSSRSVV NMEWDKIWSF
NKKVIDPVAP RYTALLKDAV VPVNIPEAQE EMKEVAKHPK NADVGLKPVW YGSRVLIEGA
DAETLTEGEV VTFINWGNVI ITKLNRNSSG KIVSIDAKLN LDNKDFKKTT KITWLAETPR
APLIPTVCVN YEHLITKPVL GKDEDFKQYI NRNSKQEELM LGDPCLRELK KGDIIQLQRR
GFFICDQPYE PVSPYSCKEA PCILIYIPDG HTKEMPTSGS KEKTKAETAK KEASSAVKGK
SAPLAGDSST PACTPSEGHL VIYNRVAAQG DVVRDLKAKK AAKEDIDKAV KQLLALKAEY
KEKTGQEYKP GNPPVPVTEQ SSKLETSGTL DSKALYDKVA EQGEVVRKLK AEKAAKEQID
EAVKILLNLK AEYKQKTGQE YKPGNPPSAP CIPSLTLPSS ECCSNLTPCS LVDGKALYDN
VAEQGEVVRR LKAEKASKDE IDEAVKLLLS LKADYKEKTG QDYKPGHPPV AQSALPQASN
AVPSGPDTPE AKALFSKVAL QGDEVRKLKS EKAEKEKIDA AVKELLQLKA QYKSVAGVDY
KPLSASGADD KDKKKKEKEN KSEKQSKQQK QNDGPKKEPL QGQSGNELSS SGSGEGQGPK
KQTRLGLEAK KEENLADWFS QVITKAEMIE YYDVSGCYVL RPWAYAIWEA IKDFFDAEIK
KLGVENCYFP MFVSQAALEK EKSHIADFAP EVAWVTRSGK TDLAEPIAVR PTSETVMYPA
YAKWVQSHRD LPIRLNQWCN VVRWEFKHPQ PFLRTREFLW QEGHTAFATY EEAAEEVMQM
LDLYAQVYED LLAIPVVKGR KTEKEKFAGG DYTTTIEAFI SASGRAIQGA TSHHLGQNFS
KMFEIVFEDP KKPGEKQFAY QNSWGITTRT IGVMIMIHGD NMGLVLPPRV ACVQVVIIPC
GITNALSEED KEALLKKCNE YHRRLLSANV RVRADLRDNY SPGWKFNHWE LKGVPVRVEV
GPRDMKSQQF VAVRRDTGQK LTFSEHEAEE RLKQILNEIQ TNLYNRASED LKRHMVVANT
MEDFQKELDS GNIVQIPFCG EIECEDWIKK TTARDQDLEP GAPSMGAKSL CIPFQPLCEL
QRGATCVCGK NPAKFYTLFG RSY
//
