ID A0A317VHC5_9EURO Unreviewed; 1327 AA.
AC A0A317VHC5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=BO94DRAFT_569023 {ECO:0000313|EMBL:PWY72438.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY72438.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY72438.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY72438.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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}.
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:PWY72438.1}.
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DR EMBL; MSFK01000033; PWY72438.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317VHC5; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000246702; 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:0019843; F:rRNA binding; IEA:InterPro.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
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; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing 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; IPR007109; Brix.
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; 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; PF04427; Brix; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SMART; SM00879; Brix; 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; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50833; BRIX; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000246702}.
FT DOMAIN 1030..1242
FT /note="Brix"
FT /evidence="ECO:0000259|PROSITE:PS50833"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 947..1004
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 149890 MW; 102D23CFE4662723 CRC64;
MAQPSAPQNP TGEPKAPVAD VPPQADDQLR NQDASAVTQP AEGQKVKSEK ELERERRKAE
KAKKFAEKQA KQAAAAKTAA PKAEKKPKIE KEKTTDAYDP KVIEAGRYEW WEERGLFQPE
FGPDGKVRPE GYFVIPIPPP NVTGALHMGH ALTNALQDTM IRWQRMKGKT TLWLPGMDHA
GISTQSVVEK MLWKMEKKTR HDLGREALVD RVWAWKKEYH ANIKNALRRV GGSFDWTREA
FTMDPNLSAA VTETFVRLHE EGIIYRANRL VNWCVALNTS LSNLEVENKE VDGRTLLDVP
GYERKVEFGV LTHFCYEIDG TKERIEIATT RPETMIGDSG IAVHPDDQRY KHLIGKFARH
PFVDRLMPIV ADKDVDPEFG TGAVKITPAH DFNDFNRGKA HNLEFISVLN DDGTFNSKGG
PFAGMKRFDA RYKVIELLKE KGLYVKWENN PMKIPRCAKS NDVIEPILKP QWWMKMESLA
KPAIEAVEKG DIVIKPESAE KSYYRWMTNI NDWCLSRQLW WGHQAPAYFV KIEGEDGDDS
DGNLWVTGRT EEAAREKAEA KFPGKKFTLI RDPDVLDTWF SSGLWPFSTL GWPRQTHDLE
NLYPTSVLET GWDILFFWVA RMIMLGIKLT GKVPFKEVYC HSLIRDSEGR KMSKSLGNVV
DPLDVMEGIQ LQDLHAKLLV GNLAEKEVAA ATKYQKKAFP KGIPECGADA LRFSLVSYTT
GGGDIAFDIQ VIHGYRRFCN KIYQATKFTL EQREFSQSAQ IVYQYWYGQL CDVFIENSKF
LLAPEVSAEA QQSAKETLYT ALEGALTLIH PMMPFVTEHL WQRLPRREGD ATISIMKAKY
PEYTPEFDDV EAETAYELIL DTSKAVRSIL AQYEIKTKGD IVIHTYDAVS HKTVSEELTS
IKSLGGKTLG DLSVLGPETT APPSGCVVAP VSSQAAVYLR VSKEVALEQE GKAKASLEKA
RETVRRQQTL ITSAGWEKAK PEVREAEQKK LLDAESEAAR LEEQIRDKPK NARTARILKA
KEPQLIEPPK RTLLLHGSKC PQPLHTVLKT IHSLTRPNSI LFHKKNEIRP FENAESLEFL
AEKNECGLVV FGSSNKKRPN CVTLARVFNT KVLDMCELLL LPREGQEEGL DSLQIGIGMR
PMLLFAGSPW EDETSTAHVM LKSMFVDMFK GETSDKIDVE GLQYVLMIGA EEPTEGLAPV
IHLRWYKLRT KRSGHKLPRV ELDEIGPKFD FKVGRMQEAE SQVMKEAMKQ GKRPNEEIKL
KKNIGLDSIG DKIGRVHLGK QDLGGLQTRK MKGLKRRAGV ESDEEDADMM DVDEISEDEG
RKRTKTA
//
