ID V5DGS5_TRYCR Unreviewed; 745 AA.
AC V5DGS5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN ORFNames=TCDM_04713 {ECO:0000313|EMBL:ESS66606.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS66606.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS66606.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS66606.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000422};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESS66606.1}.
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DR EMBL; AYLP01000042; ESS66606.1; -; Genomic_DNA.
DR AlphaFoldDB; V5DGS5; -.
DR EnsemblProtists; ESS66606; ESS66606; TCDM_04713.
DR VEuPathDB; TriTrypDB:TCDM_04713; -.
DR Proteomes; UP000017861; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd04323; AsnRS_cyto_like_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 1.10.8.1290; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:ESS66606.1}; 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:UP000017861}.
FT DOMAIN 501..737
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 262..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 84595 MW; D5EA623C33ED6E56 CRC64;
MAFRLIFERR LAPVSNSCRR CCRTMFSGPT PRITSVMRSG LRGYVLWQSP PHGSCICPAL
SSSRAFIYLP ERTTMASSEE LLESLQRIVG LDEKNSKDLS TKPERVQDLL GFFANQNMTP
ESPREQKVML FNLWAKVKLP KHRDLLADYV KRKKLDSTQK VDAAIRFVDA MKEDALFDAA
KFEKECGVDV VVSKDDTLRL VKTALAEEDL KALKTSWVKN PNMLLGKMKR VPGLQWADFT
LVKAILEELV PPMIKDVVID EAEPKTEEKT TTPPRTKGAE VAATQKCPRN ADWKCVVDLH
SLHRIGDLSS MQEGTKVRVV GWAHRVRHQS RLSFVVLRDG SGYIQAVFNG ETEPFHRETS
LAIRGTLKYE PKAATELQPP YELHVDEYAI IGNSDGSIEN AITPESSPDK LLDDRHLVLR
GTYGSTTIKV RHELIRAFRE YCWSVNMFEV TPPTLVQAEC EGGSTLFDVI YYGTTAHLTQ
SSQLYLETCT SSVGDVYCIL PSYRAEKSKT RRHLSEYTHL EVEYSICDFE LFLSKLEDLI
VGAFNRTIER AGDLIAFMNP EQMVDPKANP RDPSNWKFAP KKPFRRLKYA DAIKLCNDNG
ILNPETNAPF QFGDDITDQP ERAMVAILGE MVFMTHFPAV MKSFYMARDP EDPTLTESVD
VLAPGIGEIV GGSMRMWDHE ELIEAYRRKD LDPSVYYWYT EQRKYGSTPH GGFGLGVERF
LVWLLNLDSV REACLFPRYM GRCKP
//
