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Database: UniProt
Entry: A0A0N5CMW1_THECL
LinkDB: A0A0N5CMW1_THECL
Original site: A0A0N5CMW1_THECL 
ID   A0A0N5CMW1_THECL        Unreviewed;      1484 AA.
AC   A0A0N5CMW1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   24-JAN-2024, entry version 32.
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=TCLT_LOCUS1503 {ECO:0000313|EMBL:VDM96983.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000150201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000150201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM96983.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; UYYF01000198; VDM96983.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5CMW1; -.
DR   WBParaSite; TCLT_0000150201-mRNA-1; TCLT_0000150201-mRNA-1; TCLT_0000150201.
DR   OMA; WWFNVIL; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; 3.40.50.620; 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; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; VALYL-TRNA SYNTHETASE; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF03901; Glyco_transf_22; 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; 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   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1068..1089
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1145..1176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1188..1206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1241..1262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1268..1285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1292..1313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1319..1344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..670
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          715..863
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   COILED          924..951
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1484 AA;  171989 MW;  1C6E8470E4477546 CRC64;
     MISRSRFKYV AHMHSYYAGR GSSFQARTAN TSFDIDVVTN SYGKKARHDT VVIRSKKISP
     EVYRMVLPPP NITGNLHIGH ALTVTVEDAI CRYRRLRGQQ VTWYPGFDHA GIATQVVVET
     MLWNKMKLRR HEVTQSYFLE LCRKWKQEYK NIGRTFVRFR RVNDISKQLK ALGATLDWHN
     VYYTLDDKFS EAVKIAFCQL YDKGIIFNDL RMINWCPTLR SSISDQEVNI VDVGKSKSLG
     CVMYGCQRNL TDVGIMHLIR YELLSGDSFC GNNYLEVGTT RPETLFDDIA LAVNPNDERY
     AKHIGSHVRH PFFPNRLLPV VADLLVNINK GTGVLKVAPT HGLIDFQIAK KHKDFINDED
     LNRSCIDESG RLINTSDFDG IDRFEARRKI IDKLSACNKY GGTIPYPEHQ LKICSRTGDV
     IEPMVKKQWF MNCVDMNNRA LEAIENGVIT IAPKSMQIHL ENWLSKKEPW CLSRQLDWGQ
     QIPAFRVDPN SEWIVALDKV EAQRACGRRI TEIDLEQEKD VLDTWFCSAL IPIVLSGWPK
     KEIKYVPLTM LETGFDIAGF WVARMITVCH SLTGYWPFSQ VLLHGLVRDE NGKKMSKSIG
     NIIDPMDVID GISIQKMLER LNESNISEVE KKTASISLQS RFPKGIRRCG PDALRFALLR
     HDVTATDINI DIVQTAEEGL RFCNKLWNLC AYAKKLWESC REEALDDLSV HRIEDRWIQS
     RLESSLMVMT KKMESNSLHL AFNALHKFFC NDLCDVYIET TKKALWRKEH LRLKVIAENL
     HDIIEKSLVH LSIFMPFISE YLFDNIKRNE EQSVYNYLSE RHLKFYKIDK KLEEDMSFVL
     ELITAVRSIR SHFHIAAKNP LKVSCQTESC DLKNFESMIY ELCNVTLRMT DPEKCNNHYI
     PFPLRGYSTE INVFIEDTFG SLIKTELLRR LQKAQKRKNQ FLHRVEKHQK LAKSVVKNNS
     VECHERKIFQ AKAVVNGMEE EILKLENLIK QSMDIKGNFK DLLLAVVCVF HITIAPYTKV
     EESFNVQAYD HHKFPGVVPR TFTGALALSA PLLPVVHIFE YFNISKYWML YGMRLVLGLS
     VLFAFIEFIK RIDKQFGQLS GDFLRLLTAT QFHFMFYCSR PLPNIFALYG GKIFWTYQKI
     LDRHWICAAG IATVFTLLFR CELILFYACI FFYPILTRKF SLFSWNGAVV YCCFVAFLAL
     GISIPIDSYL WRRWLWPEGE VWWFNVILNR SKEYGVLPFS WYFYSAIPRA LSVSCVFVPI
     GLISDRRLAP IVTPVLLYVL LYSFLPHKEL RFIIYAIPIL NVSVAVCYAR IWISRRKSLF
     RMLLAVAVLV NLLLNIICTA AFLFASSKNY PGAEALVSLQ HMQRSDHNKP VSVYIDTYAA
     QTGVCRFLQL YDTWEYNKTE NLKSSQMERF DFLILGSYTE SDITNFTTLQ FHSTHQILHS
     VKAFQGIELQ RLYLLPYYWP VVKFRTQLVV MEKILIVTVV HVVV
//
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