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Database: UniProt
Entry: A0A091PGT2_APAVI
LinkDB: A0A091PGT2_APAVI
Original site: A0A091PGT2_APAVI 
ID   A0A091PGT2_APAVI        Unreviewed;       448 AA.
AC   A0A091PGT2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=Asn/Gln amidotransferase domain-containing protein {ECO:0000259|SMART:SM00845};
DE   Flags: Fragment;
GN   ORFNames=N311_02510 {ECO:0000313|EMBL:KFP90665.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP90665.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP90665.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP90665.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000924};
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|ARBA:ARBA00005306}.
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DR   EMBL; KL388183; KFP90665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PGT2; -.
DR   Proteomes; UP000054244; 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   Gene3D; 1.10.10.410; -; 1.
DR   HAMAP; MF_00121; GatB; 1.
DR   InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR   InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR004413; GatB.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
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   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE   3: Inferred from homology;
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:UP000054244}.
FT   DOMAIN          297..446
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP90665.1"
FT   NON_TER         448
FT                   /evidence="ECO:0000313|EMBL:KFP90665.1"
SQ   SEQUENCE   448 AA;  50505 MW;  0CFEA73AA7D8E0B8 CRC64;
     VLNRRCVEAA VMTGLALNCS INKKSLFDRK HYFYADLPAG YQITQQRVPI AVNGSLSYSL
     CIDNKMSHMV TKTVRIKQIQ LEQDSGKSLH DDTRSQTLVD LNRAGVGLME VVMEPDMCCG
     EEAAAAVKEL QLILQTLGSS QAVMAEGQLR VDANVSVHHP GEPYGVRTEV KNINSMRFLV
     KAVDYEIQRQ IEELENGGTI LNETRAFDSK LGCTVPMRDK EGKQDYRFMP EPNLPPLILY
     DAKSLPANMN HQQVVNIDWI HERLPDLPSV KRAKLVEQYG ILPEHSFTLL NEDGLTEFFE
     NVVKQTQMKP KKVIGWILKD LLSYLKQHSL TVKESPVSPF LLADLLNLLE KKEISSTAAK
     QVLMELWKGE GKTPLEIIKE KKLELIQDQK ELEQICQAVI DGQENEVTAI KAGNRKVLNK
     LIGLVQRETQ GRSNPVLVKQ LLEKKLSE
//
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