ID K9IVV5_PIG Unreviewed; 476 AA.
AC K9IVV5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Tryptophan--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00013782};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN Name=WARS1 {ECO:0000313|Ensembl:ENSSSCP00000049002.1,
GN ECO:0000313|VGNC:VGNC:94891};
GN Synonyms=WARS {ECO:0000313|EMBL:JAA53775.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:JAA53775.1};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000049002.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000049002.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAA53775.1}
RP NUCLEOTIDE SEQUENCE.
RA Dawson H.D., Chen C.T.;
RT "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT Sequencing.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HDB77028.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000049002.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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}.
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DR EMBL; DQIR01221551; HDB77028.1; -; Transcribed_RNA.
DR EMBL; DQIR01223451; HDB78928.1; -; Transcribed_RNA.
DR EMBL; DQIR01245482; HDC00960.1; -; Transcribed_RNA.
DR EMBL; DQIR01252701; HDC08179.1; -; Transcribed_RNA.
DR EMBL; DQIR01267158; HDC22636.1; -; Transcribed_RNA.
DR EMBL; GACC01000032; JAA53775.1; -; mRNA.
DR RefSeq; XP_003128776.3; XM_003128728.5.
DR RefSeq; XP_005656526.1; XM_005656469.2.
DR RefSeq; XP_013844693.1; XM_013989239.1.
DR Ensembl; ENSSSCT00000065002.3; ENSSSCP00000049002.1; ENSSSCG00000002516.5.
DR GeneID; 100515390; -.
DR KEGG; ssc:100515390; -.
DR CTD; 7453; -.
DR VGNC; VGNC:94891; WARS1.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_032621_0_1_1; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 540846at2759; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000002516; Expressed in caecum and 42 other cell types or tissues.
DR Genevisible; K9IVV5; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd00936; WEPRS_RNA; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Proteomics identification {ECO:0007829|PeptideAtlas:K9IVV5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 13..69
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
SQ SEQUENCE 476 AA; 53690 MW; 36BE4E7592FEE36E CRC64;
MADVPNGEQG CSSPLELFNS IAAQGELVRS LKARHAAKDE IDSAVKMLLS LKMSYKAAMG
EDYKADCPPG NRAPGIDSGL DATEAGDDFV DPWTVQTSSA KGIDYDKLIV RFGSSKIDKE
LIDRIERATG QRPHRFLRRG IFFSHRDMNQ VLDAYENKKP FYLYTGRGPS SEAMHVGHLI
PFIFTKWLQD VFNVPLVIQM TDDEKYLWKE LTLEQAHGYA VENAKDIIAC GFDVNKTFIF
SDLDYMGMSP GFYKNVVKIQ KHVTFNQVKG IFGFTDSDCI GKISFPAIQA APSFSSSFPQ
IFRDRTDIQC LIPCAIDQDP YFRMTRDVAP RIGYPKPALL HSTFFPALQG AQTKMSASDP
NSSIFLTDTA KQIKTKVNKH AFSGGRDTIE EHRQFGGNCD VDVSFMYLTF FLEDDDRLEQ
IRKDYSSGAM LTGELKKVLI EVLQPLIAEH QARRKEVTDE VVKEFMTPRK LSYDFE
//