GenomeNet

Database: UniProt
Entry: C1GNL2_PARBA
LinkDB: C1GNL2_PARBA
Original site: C1GNL2_PARBA 
ID   C1GNL2_PARBA            Unreviewed;       396 AA.
AC   C1GNL2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE            EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN   ORFNames=PAAG_00107 {ECO:0000313|EMBL:EEH35784.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH35784.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH35784.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000107};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN293992; EEH35784.2; -; Genomic_DNA.
DR   RefSeq; XP_015700243.1; XM_015843908.1.
DR   AlphaFoldDB; C1GNL2; -.
DR   STRING; 502779.C1GNL2; -.
DR   GeneID; 9101054; -.
DR   KEGG; pbl:PAAG_00107; -.
DR   VEuPathDB; FungiDB:PAAG_00107; -.
DR   eggNOG; KOG2713; Eukaryota.
DR   HOGENOM; CLU_029244_1_3_1; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 179020at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR   NCBIfam; TIGR00233; trpS; 1.
DR   PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059}.
SQ   SEQUENCE   396 AA;  43878 MW;  4C27D7002C5F722A CRC64;
     MSAAFQRTRL GHSVRKISHL CQQLSSSPSQ IPQKLQRIVS TSTTVNPPAS GGRIIFSGIQ
     PTGVPHLGNY LGALQQWVRL QNEALHSTKL IFSIVDLHAL TVPQDPSILG QCRKQMLAAL
     IAVGIDPKRS TIFFQSAVSA HSELMWILST ISSMGYLSRM TQWKSKLQLP KDSTLENSTA
     RSRLKLGLFS YPVLQAADIL VHRATDVPVG EDQKQHLEFT REVANGFNHI YGPVLTMPSA
     LISPAKRVMS LKQPTLKMSK SHSDPRSRIL LTDSSEEIHL KIKLALTDSH QEISYDPINR
     PGVSNLIEIL SHVQGRDGIS SFEELGAEYQ SFTMRAFKEH VAVVVVDHLN GIRQRYLELM
     NNKLSYLDTV AEEGAKSATE NADTTLRTVK NALGLF
//
DBGET integrated database retrieval system