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Database: UniProt
Entry: A0A077YX33_TRITR
LinkDB: A0A077YX33_TRITR
Original site: A0A077YX33_TRITR 
ID   A0A077YX33_TRITR        Unreviewed;      1614 AA.
AC   A0A077YX33;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN   ORFNames=TTRE_0000029701 {ECO:0000313|EMBL:CDW52038.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW52038.1};
RN   [1] {ECO:0000313|EMBL:CDW52038.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW52038.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594}.
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DR   EMBL; HG805814; CDW52038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077YX33; -.
DR   STRING; 36087.A0A077YX33; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF111; VALINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1115..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1253..1271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1277..1303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1315..1338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1366..1390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1419..1436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1448..1474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..117
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          186..780
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          829..976
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1614 AA;  184602 MW;  5CB6DC7D5FEF33EF CRC64;
     MNCEVSYLHR ADGSCIYTQG KTTVIASVNG PGDLKNLKQC ADSAVIQVVV KRSIGGNSAA
     NAQTAFILEN LCTSAVIVSL LPKTLISIVV QELESDGSFL QAAVNAVCLA LIDSGLPMFD
     TFAAATVAIL PQSENIIPSP SSQVERDAEC LMTAVFLHHQ PGDLFYCWSR EAAPATYDSK
     FVQNGWYDWW LRNDFFNPAP STDKHPFVMC MPPPNVTGTL HMGHALMLAI GDCIVRSHRM
     CGHHVSWIPG FDHAGLATQL VVEKHLFNSE GLLRKNMSRQ DFVTACEKWS SEKMVAMRKQ
     MESIGCSCNW KRCFYTLDQK FSIAVVEAFR RLHKDGLLYR DYRVVNWSPL LQSSISDAEV
     DVKSIDQPTD IPVPGRTKAV SFGYLYFINY PIADSSNGQS ITIATTRPET MLADEAIAVH
     PADSRYSSLV GRHVRHPLLT NRLLPVIADA QVDRDVGTGA VKVTPSHSRA DFEIARAHGL
     SLEKRCIDAS GHIISPELPE LDGLNRFECR EKIVRWLIDR DLLMDCRSHV TNVPMCRRTG
     DILEPVPKEQ WFLRCDSMAE RTMALLPRIH ILPEGMRNEW KNWLSHRVDW CLSRQSWWGH
     RIPAYRQKLD LVSSLLFYAK SYFRATFSDG SSRWVIAADE HEAGSQLERH SHSLINLAAD
     EDVLDTWFSS ALIPLVIAGW PHNWQADNDH LFPLSLMETG HDILGLWVTR MAMLSLQLTN
     RLPFSRIFFH GMVRDSEGQK MSKSRGNVVD PLKLIEGDQE TRIGADALRI SLLRSNPKGD
     TVTLDEAVRQ HSRRFCNKLW QSFKYLTKLW NKTEIPLPLK PEPYDSPVDR WILSRLSSLV
     IDVHESLEAY NFHLSVEALV NFWWLDFCDI YLEWSKHFFY PKDHLAAAEH MRCMLAMIAS
     TYLRLLAPYM PYLAEELYSL LPMADKAVSV HCAPYPTPSE VNFLDPHLEM QMRFVRDLVH
     QIRSLRRDVE VSMPIPLVAV AWCNGIQRSA IENFGRLMQR LVEFRCSLND SAEHVPPENS
     IMLVSQEECR IYVQLKNVKY EEVLKRFDRQ LEVLERKRTK LTNWMQAKRL HVSPEEAAKK
     VTQYLNDIQT VDEEMEKLRR FRRDLHRHHE HAKMLLGLLR VLTFVIMLYY AVLIPFTKVE
     ESFNMQAVHD ILFHGFNLSK YDHFEFPGVV PRTFIGPLYL AGIVFPLRLL DYPIKFSKPY
     LQLCTRLALG ATVCFGHVRL SRSLKLAFDL NVACWYMAIT LSQFHTMFYA SRTLPNIFAL
     ALFLFVVAFY LDGRYYMAAI VATFSATVFR LELAILYAIM FFPILSKWRR RGVKLACIVL
     LTGIGFVALS TVIDSYFWNR LVWPEGTVWW YNIVLNKSSN WGTLPFFWYF YSAIPRNLCF
     TLCFVPFALF GPEKIRRLTV CALGYVLIYS FLPHKELRFI FYAIPLLNMA ASWVSARMML
     MRSSSVPTLI GISLSLVQPM INMLLALCFM RAAIANYPGG EAIVTLHTTL RAEGLSGKPV
     RIHIDSYCAE TGVTRFLQVN PLWEYNKSES LILPEQKIDF DYLLIGDSDD VTQVNKNYIT
     THRTLYFFHG FAGIEIERNA TFPFLTVQYK LKPRVALLKK EPLITTTVEP VVEA
//
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