ID A0A0V0RPI1_9BILA Unreviewed; 2143 AA.
AC A0A0V0RPI1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:KRX16372.1};
GN ORFNames=T07_14325 {ECO:0000313|EMBL:KRX16372.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX16372.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX16372.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX16372.1};
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:KRX16372.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDL01000108; KRX16372.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RPI1; -.
DR Proteomes; UP000054630; 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 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; 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:KRX16372.1};
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:UP000054630};
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 1647..1666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1706..1725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1731..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1759..1778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1819..1847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1854..1872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1907..1930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1936..1953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1960..1979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1991..2010
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 1559..1593
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 53..81
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 2143 AA; 246205 MW; 1A539E9F62ABAEA3 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 LPNHHRNRSY SRMLKKQPLK NHTDQRMREK KMSNNVTELE
AEFRCTVRYV EDCTGSCLVS KRGTTLLISV HGPTDVKASK QLPDSAVVQV HLTTVSKDEI
GGRSSIDSGQ MTLFLQNICQ SIILVKLLPK RLITVVVQEL ESDGCFMEVA VNGLCIALLE
SALPMNDMFA ASTLAYYGGA SGQILLNPTA KEETEADCVL CCVYLDHVVE NVFSIWTKGN
MPLSMLDQVL SQAETQSHML LIGRRWMWSI FWRKLATRPD KGERPAAYDA KFVESCWYDF
WLANDFFNKS PTSRRRPYIF CLPPPNITGD LHLGHALTVA IEDAIARKYR MCGDAVFWIP
GFDHAGLATQ LVVENMLFNK NGILRKEMSR EDFVRACDVW KTERMASIEN QLIKLGSSLS
WQRTFYTMDT NFTKAVVEAF KILHQQGLIY RDYRIVNWSP YFCSVISDIE VQLRYVEQPT
EITVPGRIEP VSFGRMYFIK YPLENSTAED EFVIVATTRP ETIPADQAIA VHPEDPRYGH
LIGFRVRNPL LPGKLLPVIC DKRVEQNLGS GVVKVTPAHG RMDFDIAREH GLPLEHRCID
DQGRMEVEEL VELDGLERFT GRELVLSMLI NRDLLVDCKS HPMNVPICIR SGDVVEPMLK
EQWYLDCSEL ATEVKHAVDR LDILPAGMRN EWINWTSKSE DWCLSRQSWW GHRVPAYYAN
FESDCHPSVW VVASDETDAR NVIADKYPQY TLANLRQDDD VLDTWFSSAL VPLVLGGWPE
KFRSDFTENC YFPLSLLETG HDILGFWAVK MAMLSLQLVG ELPFRKLLLH GMICDERRQK
MSKSKGNVIN PMQLIQGTPS TETDKGTTAY GADAVRFALL RSNVKADTVA FDKTMLTRSR
HFCNKLWQSF KFLKKMWNND AQHEYTSVVD KWILSRLSAV VKNVNESFET YDFHRCTNDL
LDFWWFEFCD VYLEWSKHYF YPQRCPTAEN IVSIFATVTD TYLRLLAPFM PFLAEELYSM
LPLENKAISV HDAAYPKTDT INFFEPHLDS QMRFISELLH HVRSVRREFN ICPGKPLKGI
AACKGVERAA LENFSDLIHQ LAGFRCDLVD SDKCNIRMRN NYLTLISQEN CQLHMKLMYV
NQDEILERFE RQLNSLQKKR EKLLKKLNTV GREQTDNERC AAASQHLKDL IALDSEIQKF
QSFKHRIQSF LHRMRLLRWL SYFRRDYLIT FTLLPYVISI VSILLIPCTK VEESFNLQAV
HDFLYHRTDL KSYDHNYFPG VVPRTFIGAL LLSVAVYPFY ILAQLFGLSK FWLLIATRCM
LTTGVYIAYY KLLKSASRVC SLAGAYNMAL FGAFQFHFTF YSSRTLPNTF ALIFAVKSST
DKIILLTLSK LLDEDYKKAI FFGAFTVVVF RSETAILFAL LFCGFAFESR DRILSTLFYG
ILAIAFSVVV SFTVDSVMWG KAVLPELTGF VFNVIRGGSS NYGTSPFFWY FYSALPRALG
PVSLLVPFTF GDRNPVGWFA FSAIGYVFVY SILPHKELRF IIYTVPIFNL AAGYAAAKYR
LHPIASFGSF LYRRLVQLGV IGTLIMEVLF MTAASYNYPS CAALNVVDEI AQLKYAHSSE
ITVYIDSFCA QNGISRFLQT NKHWNYQKEN DGLDLETVKR FQFLLIGHET HLHNEIRPFL
DTHRVVKFLP GYAGIGLNYT TFGRLPGLYF KKRDKVAILE KLR
//
