ID   A0A261CC43_9PELO        Unreviewed;       470 AA.
AC   A0A261CC43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit B/E catalytic domain-containing protein {ECO:0000259|Pfam:PF02934};
DE   Flags: Fragment;
GN   ORFNames=FL83_05709 {ECO:0000313|EMBL:OZG19630.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG19630.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG19630.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG19630.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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:OZG19630.1}.
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DR   EMBL; NIPN01000020; OZG19630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261CC43; -.
DR   Proteomes; UP000216463; 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; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
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:UP000216463}.
FT   DOMAIN          103..285
FT                   /note="Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit
FT                   B/E catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02934"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG19630.1"
SQ   SEQUENCE   470 AA;  54005 MW;  758C5A435CCE91FA CRC64;
     MDTHEKCGDG DSRHPRATEH THQTVLPVSN KRRVAKLSCL PIRHGHTGHS PRLESSMCSS
     CTEDVTSSEV SRSEMVTIRS ETLFLCGHAG GLSDYTKRTS HREGWTVEIV QLQLEQDSGK
     TINIVDSDSP ESPESRSLID YNRAGCALIE IVTSPCFETA IEAIRFVQTL RLLIIHHNLS
     DGELHRGHLR VDANVSLTVD GKPGTRTEIK NMNSIRTIHT AINFEIARQF EILSNSSGKV
     IRETRGVDSE GRTVRMREKD AEDTDYRFMV EPNLPILKIR KEWMEGAERE LETQGIADFE
     WLRDRCEPDL LAFVKRCVRF KDSGVTADEI LYWMRELKTI MQRSKGNYPP KSDFFAKQFT
     TLIHHSGRLT RLRLLDLLRF YATSSESEED VLLEDVMEFI DKNEFWRISD TEKIDKFVEE
     SMAKNGKLAE KVRSGHAKSF NKMRNLMIET SEKRIELEDA EDAIRRFLQR
//