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Database: UniProt
Entry: A0A0W0FGU5_9AGAR
LinkDB: A0A0W0FGU5_9AGAR
Original site: A0A0W0FGU5_9AGAR 
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}.
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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
//
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