ID A0A1X2IXR6_9FUNG Unreviewed; 988 AA.
AC A0A1X2IXR6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BCR42DRAFT_486417 {ECO:0000313|EMBL:ORZ24098.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ24098.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ24098.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ24098.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORZ24098.1}.
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DR EMBL; MCGE01000002; ORZ24098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IXR6; -.
DR STRING; 90262.A0A1X2IXR6; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000193560; 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; 3.90.740.10; 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; 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; 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:UP000193560}.
FT DOMAIN 108..732
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 777..927
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 111235 MW; C42B3E6174868DD8 CRC64;
MAAEQPTKEV PPQLTEEAAA AAAAKKAKNE AKNEEKRQAK LAKLAAKQAK LEEQKKKAAS
SENAEKKKKK AAKAETPVFV NKTPKGEKKD MSEPMASTYD PRAVESAWYE WWVKEEYFKP
ELTEDGQIKP EGSFIVPAPP PNVTGSLHIG HALTVAIQDT LVRWNRMLGK TVLFNPGTDH
AGISCQSVVE KKLWAESKIT RHDLGREAFV DKVWEWKEKY GGRIHDQFYR LGASYDWDRA
AFTMDPKLSK AVRETFVRLH REGTIYRANR LVNWCVRLNT ALSNLEVENK EIAGRTLMNV
PGYEANEKFE FGVLNEFAYL VDGSDERVVV ATTRIETMLG DSAIAVHPND ERYKHLHGKF
VVHPFLNRRI PIITDDIAVD MAFGTGAVKM TPAHDFNDYE VGKRHNLEFI NLMNDDGTFN
ENAGPYAGMK RFHVRTKIIE DLKAKGLFVD VKDNPMTVPV CSKSGDVIEP VMKPQWWVNC
KPMADAACQA VRDGKLKIAP KVSEGDWFRW LENIQDWCIS RQLWWGHRVP AYYVVMEGST
PDYSDDAHWV SGQDEAEARA EAERKFPGKK FTLEQDPDVL DTWFSSGLWP FSLMGWPDKT
DDMMKFYPSS LLETGWDILF FWVARMVMFG IKLTGEVPFT EVFCHAMIRD AHGRKMSKSL
GNVIDPVDVI EGITLEGLHG RLLEGNLDAK EVEKAKSGQK ADFPKGIPEC GTDALRFALC
AYTTGGRDIN LDILRVEGYR KFCNKIWNAT RFAMMKLGSD FKPVESFKAS GDESLADKWI
LHKLNKAAVE ANKGLSERNF LAATNAVYQF WLYELCDVYI EVIKPVCDMD TTNDETAARR
KTTAQNTLYT CLEAGLKLLH PFSPFVTEEL YQRLGRRPGD VTPTIVKAKY PVNEPTFVNE
AAAKQFDIVF EATKSIRSLA VQLNKKKEGV AFVHAGNNDL HELLSAESPS ILALARGIKD
LTVSIKGDAP ADTEAAEVNV DITVYLQK
//
