ID A0A0W0FGU5_9AGAR Unreviewed; 466 AA.
AC A0A0W0FGU5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit B/E catalytic domain-containing protein {ECO:0000259|Pfam:PF02934};
GN ORFNames=WG66_11729 {ECO:0000313|EMBL:KTB35564.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB35564.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB35564.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB35564.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB35564.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATX01001986; KTB35564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FGU5; -.
DR eggNOG; KOG2438; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR004413; GatB.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR NCBIfam; TIGR00133; gatB; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS01234; GATB; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 11..296
FT /note="Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit
FT B/E catalytic"
FT /evidence="ECO:0000259|Pfam:PF02934"
FT REGION 427..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 52246 MW; E92403FA391B8E1D CRC64;
MSRLILDGWQ VVIGIETHVQ LKTRQKLFSR ANTSLLSHSP NSRHNAFDAA FPGTLPKLNP
KCLDLAVRAA LALNCKVQNR SSFDRKHYFY SDQPVGYQIT QHYAPFALNG FLKPPKLDLP
VRIKQLQLEQ ACLLDTGKSI YNARSRISSI DLNRAGTGLL EIVTEPDLSS PEEAAEYVRS
LQSTLRAMGV SDGNMEAGDL RCDVNVSMNR PGEARGTRCE IKNLNSVRFM VAAIHHEIER
QKGILSSNSS VLQETRGFDE NRFETYTIRS KEDAPDYRYM PDPNLGVLIV NDTTIERIRK
SLPESPEAMR TRLLTTYGPH GVNNASIDVL MGLDASRDVP FDGEVSSQQE SAVPYFEVLA
QGRDPREVVN WYDNSDFVGT AFVSESNLLT KALIGSPDGR THRPGHFRED DQIVWKTPFT
PRSNEPFTFS AHEGNGNSSR PDRIRGRGGY RPIYGDMFSS DRRPPI
//