ID A0A182M3J8_9DIPT Unreviewed; 1122 AA.
AC A0A182M3J8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|ARBA:ARBA00024407};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA008589-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA008589-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA008589-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; AXCM01002234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182M3J8; -.
DR STRING; 139723.A0A182M3J8; -.
DR EnsemblMetazoa; ACUA008589-RA; ACUA008589-PA; ACUA008589.
DR VEuPathDB; VectorBase:ACUA008589; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000075883; 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: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; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
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; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF117; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 192..788
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 846..980
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1091..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 127991 MW; 89D0235436768E3A CRC64;
MVQGGDGVGE IVFGRIKLLD IARYFLHHVF RLFRTALDVG NEGKQLRQGL LRFLQCNSTV
FARIHLAPHH TADVIVDQTY VAFHLGYHLI DVGERLFVRK QLVDVIGRIE IRLVERVGTL
QHLFDRTLNV FRQDDFVDVI LFLVIFFLDQ YSDEFREDNS IDIASAYQPS QVERHSTSGT
VPQLPAELRS VEKVDAPFNL LLPPPNVTGD LHLGHALTCA IQDALVRQAR LSGARATWIP
GMDHAGIATQ VVVEKRLFKE RNLTRHNLGR EMFLEEVMRW KVEKEESIRM ALKKLGCSMG
WSKEYFTMDS QQSVAVREAF VQLFDKGLIY RDRSLVNWSC TLESAISDVE VENVEIAGPT
EISVPGYDRN ITFGRMVDIA YKVQGSTEEI VVSTTRPETF LGDVAVAVHP EDGRYSHLRN
KVIFLWHPVR KEEIPLIFDS AVDRTFGTGA VKITPAHDRF DFEIARRHHL ATVEVIDERG
IVQKHFGPFT GLPRYDAREK VIDYLTKLSL VRGVKPHTML LPLCSRSKDV VELLLRPQWF
IRCQEMAQRA LAAVRDDGSL AIVPKTFERE WFRWLENCHD WCISRQLWWG HRIPAYVARY
ETTKELWIAA RSMNEAREKC AKLLPNVPQD AISIEQDHDV LDTWFSSALL PFSSTGWPDK
LSTEFYPLQL METGHDILFF WVARMVMLGQ ELTGQLPFGK ILLHGIICDE FGRKMSKSLG
NVIKPEHVIH GITLDKLHAE AEASHRQGIL SKHELSKSIA GQRKMFPKGI PECGIDALRF
TLCSSNVKNH FIHFNVQEAF TNKLFFNKIW QATRYTLGCT ERFGVSQRAL RTAELREAAD
QLTSMDRWIL SRLGNTVQQC REAFESYNFH LATAALRTFF YNNFCDVYLE TTKINMKPER
TKAAELHCGV LKYCLTVGLL QMEPFTPYLA QELLNHLSPS STLADDWASV TGWIDPQLEE
RIDGMLQICQ HIRQSKNEYN PPIVRKHNPT VHIHAKAQEL AGLLQTQQAT VQQLTHCNGI
VLHADESTFN KVQFLVKSAP SHNCIIGIVA ESIDAATSEG QTVAGDGSKK MLAKLDAEIE
KLLKTISNEG YKKSASESVQ KRHREKLNQL QQQKEEMLKI RS
//
