ID V2WK87_MONRO Unreviewed; 459 AA.
AC V2WK87;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Glutamyl-trna synthetase {ECO:0000313|EMBL:ESK87243.1};
GN ORFNames=Moror_5808 {ECO:0000313|EMBL:ESK87243.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87243.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK87243.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87243.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007894}.
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:ESK87243.1}.
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DR EMBL; AWSO01000818; ESK87243.1; -; Genomic_DNA.
DR RefSeq; XP_007853451.1; XM_007855260.1.
DR AlphaFoldDB; V2WK87; -.
DR STRING; 1381753.V2WK87; -.
DR KEGG; mrr:Moror_5808; -.
DR HOGENOM; CLU_015768_6_3_1; -.
DR OrthoDB; 5404395at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363037};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363037};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 29..276
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 306..451
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
SQ SEQUENCE 459 AA; 51516 MW; 95AC5DCB4C16AF77 CRC64;
MVHFSCLSTS AHGLTEGLVE TGPGKDDKYG PYYQSERLDL YRTYAKKLVD KGHAYRCFCS
PDKLSSIRER LARLGSNNSY DKSCLHLSDE EVARKVKAGE KYTVRINDSN PPNRPPTHDL
VFGLVKDAHL SLATDPILLK SDGFPTYHLA SVVDDYTMNI THVLRGEEWL PSLPLHLDLY
AHLDIKPPEF AHLPLLLNSD GSKMSKRNGD VRVIDYIKRG WEPTALLNWL ALAGWGTSSS
HDAPDSTRPM PIQELESEFD LTALTQRNSS LDPAKLEYLN KWHLGTKIHN DAQGSLKELA
ERIRDNVKSQ FPVSQYTTIE NIMSAIQILD RRLVTIIDVP VLAPYLFIEP DYSTAEAADM
LQRVSGDLSR ILNSALGVVR HLVDSNQWES TPGTHMLALL NAERDNLGLT GKEKKKYMMA
LRWALTGMKD GPAIVDIIKV LGHERTLERL RVPGQKEAS
//
