ID A0A2Z6RFE7_9GLOM Unreviewed; 1063 AA.
AC A0A2Z6RFE7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=RCL2_000972500 {ECO:0000313|EMBL:GES82526.1}, RclHR1_02710018
GN {ECO:0000313|EMBL:GBB96259.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB96259.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB96259.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB96259.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GES82526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HR1 {ECO:0000313|EMBL:GES82526.1};
RA Maeda T., Kobayashi Y., Nakagawa T., Ezawa T., Yamaguchi K., Bino T.,
RA Nishimoto Y., Shigenobu S., Kawaguchi M.;
RT "Conservation and host-specific expression of non-tandemly repeated
RT heterogenous ribosome RNA gene in arbuscular mycorrhizal fungi.";
RL Submitted (OCT-2019) 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:GBB96259.1}.
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DR EMBL; BEXD01001902; GBB96259.1; -; Genomic_DNA.
DR EMBL; BLAL01000061; GES82526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6RFE7; -.
DR STRING; 94130.A0A2Z6RFE7; -.
DR Proteomes; UP000247702; Unassembled WGS sequence.
DR Proteomes; UP000615446; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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 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:UP000247702}.
FT DOMAIN 108..732
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 777..930
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 993..1056
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 998..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 120668 MW; 69FE129D847D8984 CRC64;
MDGSKEQTPS SESSQTPAET DTTPASTTAK SKNADKNEAK RQAKLAKYAA KQAKLNSTES
EKKKEKVKKP KIDKKVDEFI DITPPGEKKD MSKPMASAYN PKAVEAAWYA WWENQGFFKP
ELTPDGKPKP EGLFVIPAPP PNVTGSLHIG HGLTVAIQDT LSRWNRMLGK TVLFNPGIDH
AGISTQSVVE KKLWVEKKQT RHDLGRETFV NEIWKWKNKY GDRIHSQLKR LGGSYDWGRA
VFTMDEKPSR AVVETFCRLQ EEGIIYRSTR LINWCVRLNT SLSNLEVENK EISGRTLLSV
PGYDQEEKFE FGVLTSFGYP IENSDEKIIV ATTRPETMLG DTGIAIHPKD ERYKHLHGKF
AVHPFNGRKL PIVLDEIVVD MTFGTGAVKI TPAHDFNDYE VGKRHNLEFI NILNDDGTLN
AKGAPFQGMK RFHVREAVIN ALKEKGLYVG TIENPMTVPV CSKSGDIIEP LLKPQWWVNC
SDMAKNAMRA VEDGKLRIFP STSEKEWFRW LDNIQDWCIS RQLWWGHQIP AYFINISNQD
QDFSDGKYWV SGRNLEEAQE KANKKFPDVE FTLERDPDVL DTWFSSGLWP FSIFGWPDKT
SDLETFYPTT ILETGWDILF FWVARMVMLG IKLTGQVPFN EVFCHAMIRD AHGRKMSKSL
GNVIDPVDVI QGISLEELHA KLHEGNLDIR EIEKAKAGQK ADFPNGIPEC GTDALRFALC
AYTSGGRDIN LDILRVEGYR KFCNKLWNAT RFALMKLGDD FTPRENAKKT GEESLAEQWI
LHKLNQSAIE TNKSLYERNF MAATTAIYNF WLYELCDVYI ELIKPLTDAD TSITDNAKRK
RSAQDTLYTC LEAGLKLLHP FMPFVTEELY QRLPRRPADD IPTIIKAKYP DEEPEYHNLQ
AEEQFELIFS VIKAARSLIV EYNIQSNASL FIQAASEKIA SLLTSQEQSI ITLVKGAKSV
HVFQKGEAIP TGCALSTVND EINVLLMVKG FIDIDAEISK FEKKLDKTIQ SLTSLQKNIS
IPGYENKVPE DVREANDIKL KNYQAEIDAL THSIQNFLKL KDS
//
