ID   F4WIU4_ACREC            Unreviewed;       496 AA.
AC   F4WIU4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Putative glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000313|EMBL:EGI65890.1};
DE   Flags: Fragment;
GN   ORFNames=G5I_05619 {ECO:0000313|EMBL:EGI65890.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI65890.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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; GL888177; EGI65890.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WIU4; -.
DR   STRING; 103372.F4WIU4; -.
DR   eggNOG; KOG2438; Eukaryota.
DR   InParanoid; F4WIU4; -.
DR   Proteomes; UP000007755; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000007755};
KW   Transferase {ECO:0000313|EMBL:EGI65890.1}.
FT   DOMAIN          346..495
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGI65890.1"
SQ   SEQUENCE   496 AA;  56236 MW;  7FA5BDCDC63A8C02 CRC64;
     LTIREKWKST VGLEVHAQIA TESKLFSSAS TNFANPVNSC VSFFDCATPG TLPVLNRKCV
     ESAVMTALAL SCRLNEISLF ERKHYFYADL PAGFQITQQG QPIAVNGEIK FHVFTPGLHK
     SPYLKSSKIK KIQLEQDSGK SLHDENVARS LIDLNRAGIP LMEFVFEPDL VDGEEAAALV
     KELAFMLQLL GVCSSKMEEG ALRVDANVSV SNRDSLGIRT EIKNIGSVRA VAAAIQYEIN
     RHISILEVGD KMFNETRAWD GVNKKTIPMR EKEDKEDYRF MPETNLPPLC IHLREDLPNK
     SNLVDAVVLK RQLPELPEQI RHRLKDVLKI SPEITIALMS DFALLQLFNR ITRNNENRKP
     QLVAKFLVME LLTFLYKNKL MIEFCVSHED FIGELIDLLQ SNLINLITAK KILKKLVNSN
     KLPKEIVKEH NWFLISDEKQ LEQICLEIIE KNPKLVSAYK SGKKKLFNTL MGEMAKVTEQ
     CADMTVVARI MERLLK
//