ID A0A0B7NN70_9FUNG Unreviewed; 1295 AA.
AC A0A0B7NN70;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 Name=PARPA_14377.1 scaffold 50209 {ECO:0000313|EMBL:CEP20056.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP20056.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP20056.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP20056.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001624};
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; LN734207; CEP20056.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7NN70; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000054107; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
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:SF109; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 126..755
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 801..954
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 144588 MW; C48B51952A77E974 CRC64;
MFCTSVSSIP HMSAADTKEQ KEAPVAAAAA ATAAVELDPA AAAKKAKNEK KNEEKRLAKM
AKFAAKQAKL DEAKKNATAP NAEKKKKKEP KPPAPVFVNK TPKGDKKDMS EPFASAYDPR
AVESAWYDWW VKEGFFKPEF GPDGKPKPEG TFVIPAPPPN VTGSLHIGHA LTVALQDALI
RWNRMLGKTV LFQPGTDHAG ISCQSVVEKM LLKEQGITRH DLGREKFVEQ VFAWKEKYGN
TIHTQFERLG ASFDWDRAKF TMDPASIYAN GPSAAVRENF IRLHRDGIIY RANRLVNWCV
QLNTTLSNLE VDNKEIEAHT LMSVVGYDKN ERFEFGVLNE FAYQVEGSVE RLVVATTRIE
TMLGDTAIAV HPNDERYKHL HGKYVVHPFL DRRIPIVTDD IAVDMEFGTG AVKITPAHDF
NDYEVGKRHN LEFINLLNDN GTYNENAGPY QGMKRFHVRN KIIEDLKEKG LFVGVKENPM
TVPVCSKSGD IIEPVMKPQW WVKCQGMADK AMQAVKDGEL KIAPDFCNGL WFSWLKNIND
WCISRQLWWG HRIPAYFVKI EGEEHDSMNE DMWVVAADEE EAYAQAKSKF PGKKLSLEQD
PDVLDTWFSS GLWPFSTQGW PEKTFDMEHF YPASMLETGW DIIFFWVARM VMLGIQLTGK
VPFAEVYCHA LIRDAHGRKM SKSLGNVIDP IDVIEGITLQ GLHDKLSQSN LDPKETKKAT
AGQKADFPNG IPQCGTDALR FALCNFSTGS TDIDLEILRI EGYRRFCNKL WNATRFALMK
LGDDFVPSKS ADPSGNESLA DKWILSRLNK CAIDTNTALE QRNFMMATNN VYQFWLYDLC
DVYIETVKPI CDADTAGDEA ATVRKITAQN TLYTCLEAGL KLLHPFMPYV TEELFQRLGR
RPGRDERSIV LARYPVENEA YNKYEQAEKD FNTVIEIVKS IRSLASDLDK KKDLVAYIQT
DDSDLKSLYE DNKGSIAALV KGLVELTVSD ASAGAPADCG TAACGKNVTL FIRNRQEMAQ
PVAQKLLVVG GSGFLGLSIC KIAANKGWET VSLSRRGEPT AFSEYGKPEW AQKVQWASGN
SLEPDTYRDV LKDVTAVVHS VGILMENDYK SVAQAQSLCE AASGIPRMIL GMKDHGNPLD
PKLKNNPRPT YEMMNRDTAK TIADEVSKLP SISSFVYISA SDVFPFIDPR YITTKREAER
YLFQSKEFKT VVLRPGFMYS VSRPTAIPIA GALQFANAVA SPFKDAIASL PGGKIITTPA
LQTEQVARAV IAGIESRQAG IFDVQGIEEL SRTPI
//
