ID A0A0V1AT84_TRISP Unreviewed; 1652 AA.
AC A0A0V1AT84;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
GN Name=Vars2 {ECO:0000313|EMBL:KRY27817.1};
GN ORFNames=T01_650 {ECO:0000313|EMBL:KRY27817.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY27817.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY27817.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY27817.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:KRY27817.1}.
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DR EMBL; JYDH01000233; KRY27817.1; -; Genomic_DNA.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 CDD; cd17950; DEADc_DDX39; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 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.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRY27817.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000054776}.
FT DOMAIN 53..81
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 84..257
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 269..430
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 1581..1615
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 53..81
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 1652 AA; 189513 MW; 79CF94246A88820D CRC64;
MATLGHEELL DYEDEQEETV QHSKIADIQT DHHLEVVGGK KPVKGAYASI HSSGFRDFLL
KPELLRSIVD CGFEHPSEVQ HECIPQAILG MDVVCQAKSG MGKTAVFVIA TLQQLNAVEG
EVHCLVMCHT RELAFQISKE YERFCKYMPK VKVAVFFGGT NVKKDEDMLR NNTPHIVVGT
PGRLLALARN RVLSLKSIKY FILDECDRML GDLDMRRDVQ EIYKMTPREK QVMMFSATLS
KELRPVCKKF MQDPMEVYVD DEAKLTLHGL QQYYVKLKET EKNKKLFELL DVLEFNQVVI
FVRSVQRCMA LNELLTEQNF PSIAIHRSMA QEERLSRYQQ FRDFHKRILV ATNLFGRGMD
IERVNIVFNY DMPEDSDTYL HRVARAGRFG TKGLAITFVS DESDAKVLND VQDRFDVSIG
ELPDELDLKI VENWRRNFDE LPNHRNRSYS RMLKKPAVII ETVVKKSHRS ANGNKLTCNS
SDVKREKKMS NNVTELEAEF RCTVRYVEDC TGSCLVSKRG TTLLISVHGP TDVKASKQLP
DSAVVQVHLT TVSKDEIGGR SSIDSGQMTL FLQNICQSII LVKLLPKRLI TIVVQELESD
GCFMEVAVNG LCIALLESAL PMNDMFAAST LAYYGGASGQ ILLNPTAKEE TEADCVLCCV
YLDHVVENVF SIWTKGNMPL SMLDQVLSQA ETQSHMLLIG RRWMWSIFWR KLATRPDKGE
KPAAYDAKFV ESCWYDFWLA NDFFNKSPTS RRRPYIFCLP PPNITGDLHL GHALTVAIED
AIARKHRMCG DAVLWIPGFD HAGLATQLVV ENMLFNKNGI LRKEMSREDF VRACDVWKTE
RMASIENQLI KLGSSLSWQR TFYTMDTNFT KAVVEAFKIL HQQGLIYRDY RIVNWSPYFC
SVISDIEVQL RYVEQPTEIT VPGRIEPVFF GRMYFIKYPL ENPTAEDEFV IVATTRPETI
PADQAIAVHP EDPRYGHLIG LRVRNPLLPG KLLPVICDKR VEQNLGSGVV KVTPAHGKMD
FDIAREHGLP LEHRCIDDQG RMEVEELVEL DGLERFTGRE LVLSMLINRD LLVDCKSHPM
NVPICIRSGD VMEPMLKEQW YLDCSELATE VKHAVDRLDI FPAGMRNEWI NWTSKSEDWC
LSRQSWWGHR VPAYYANFEN DCHPSVWVVA SDETNARNVI ADKYPQYTLA NLRQDDDVLD
TWFSSALVPL VLGGWPEKFR SDFTENCYFP LSLLETGHDI LGFWAVKMAM LSLQLVGELP
FRKLLLHGMV CDEQRQKMSK SKGNVINPMQ LIQGTPSTET DKGTTAYGAD AVRFALLRSN
VKADTVAFDK TMLTRSRHFC NKLWQSFKFL KKMWNNDAQV NILSHECTSV VDKWILSRLS
TVVKNVNESF ETYDFHRCTN DLLDFWWFEF CDVYLEWSKH YFYPGRCPTA ENIVSIFATV
TDTYLRLLAP FMPFLAEELY SMLPLENKAI SVHDAAYPKA DTINFFEPHL DSQMRFISEL
LHHVRSVRRE FNICPGKPLK GIAACKGVER AALENFSELI HQLAGFRCDL VDTDKCNIPM
SNNYLTLISQ ENCQLHMKLM YVNQDEILER FERQLNSLQK KREKLLRKLN TVGREQTDNE
RCAAASQHLK DLIALDSEIQ KFQSFKHRIQ SL
//
