ID A0A0V0X8H5_9BILA Unreviewed; 2243 AA.
AC A0A0V0X8H5;
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=DDX39B {ECO:0000313|EMBL:KRX84196.1};
GN ORFNames=T06_14497 {ECO:0000313|EMBL:KRX84196.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84196.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX84196.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX84196.1};
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:KRX84196.1}.
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DR EMBL; JYDK01000008; KRX84196.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
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: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 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; IPR005599; GPI_mannosylTrfase.
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; PF03901; Glyco_transf_22; 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:KRX84196.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Reference proteome {ECO:0000313|Proteomes:UP000054673};
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 1658..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1692..1711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1746..1767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1800..1819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1855..1881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1893..1915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1943..1965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1972..1990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1996..2013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2034..2054
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 1607..1641
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 53..81
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 2243 AA; 257864 MW; F9813B53807E0B7D 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
ELPDELDVTS YSKLYYSKIK LKIVENWRRN FDELPNHRNR SYSRMLKKNS RNYRNSCNNY
SFHIVKKLHR SANGNKLICN SSDVKREKNM SNNVTELEAE FRCTVRYVED CTGSCLVSKR
GTTLLISVHG PTDVKASKQL PDSAVVQVHL TTVSKDEIGG RSSIDSGQMT LFLQNICQSI
ILVKLLPKRL ITIVVQELES DGCFMEVAVN GLCIALLESA LPMNDMFAAS TLAYYGGASG
QILLNPTAKE ETEADCVLCC VYLDHVVENV FSIWTKGNMP LSMLDQVLSQ AETQSHMLLI
GRRWMWSIFW RKLATRPDKG EKPAAYDAKF VESCWYDFWL ANDFFNKSPT SRRRPYIFCL
PPPNITGDLH LGHALTVAIE DAIARKHRMC GDAVFWIPGF DHAGLATQLV VENMLFNKNG
ILRKEMSRED FVRACDVWKT ERMASIENQL IKLGSSLSWQ RTFYTMDTVS LSHFAIQNFT
KAVVEAFKIL HQQGLIYRDY RIVNWSPYFC SVISGIEVQL RYVEQPTEIT VPGRIEPVSF
GRMYFIKYPL ENPTSEDEFV IVATTRPETI PADQAIAVHP EDSRYGHLIG LRVRNPLLPG
KLLPVICDKR VEQNLGSGVV KVTPAHGKMD FDIARENGLP LEHRCIDDQG RMEVEELVEL
DGLERFTGRE LVLSMLINRD LLVDCKSHPM NVPICIRSGD VMEPMLKEQW YLDCSELATE
VKHAVDRLDI LPMGMRNEWI NWTSKSEDWC LSRQSWWGHR VPAYYANFEN DCHPSVWVVA
SDETDARNVI ADKYPQYTLA NLRQDDDVLD TWFSSALVPL VLGGWPEKFR SDFTENCYFP
LSLLETGHDI LGFWAVKMAM LSLQLVGELP FRKLLLHGMI CDERRQKMSK SKGNVINPMQ
LIQGTPSTET DKGATAYGAD AVRFALLRSN VKADTVAFDM TMLTRSRHFC NKLWQSFKFL
KKIWNNDAQH EYTSVVDKWI LSRLSAVVKN VNESFETYDF HRCTNDLLDF WWFEFCDVYL
EWSKHYFYPE RCPTAENIVS IFATVTDTYL RLLAPFMPFL AEELYSMLPL ENKAISVHDA
AYPKADTINF FEPHLDSQMR FISELLHHVR SVRREFNICP GTPLKGIAAC KGVERAALEN
FSELIHQLVG FRYDLVDSDK CNNICMRNNY LTLISQENCQ LHMKLMYVNQ NEILERFERQ
LNSLQKKREK LLRKLKTVGR EQTDNERCAA ASQHLKDLIA LDIASSILAC MFIYYLYRMR
MLRWLSYFRR DYLITFTLLP YVISIVSILL IPCTKVEESF NLQAVHDFLY HRTDLKSYDH
NYFPGVVPRT FIGALLLSVA VYPFYILAQL FDLSKFWLLI ATRCTLTTGV YIAYYKLLKS
ASRVCSLAGA YNMALFGAFQ FHFTFYSSRT LPNTFALIFV LLTLSKLLDE DYKKAIFFGA
FTVVVFRSET AILFALLFCG FAFESRDRML STLFYGILAV AFAVVVSFTV DSVMWGKAVL
PELTGFVFNV IRGGSSNYGT SPFFWYFYSA LPRALGPLSL LVPFTFGDRN PVGWFAFSAI
GYVFVYSILP HKELRFIIYT VPVFNLAAGY AAAKYRLHPI ASFGSFLYRR LVQLGVIGTL
IMEVLFMTAA SYNYPSCAAL NVVDEIAQLK YAHNSEITVY IDSFCAQNGI SRFLQTNKHW
NYQKENDELD LETVKRFQFL LIGHETHLHN EIRPFLDTHR VVKFLPGYGG IGLNYTTFLR
FPRLYFKKRD KVAILEKLMN SKPTATFIHP YHDQMSTAFL LTLFDSFPYT ISNSKSINSP
YSEVMMEREQ VSHWNLLKPR TLL
//
