ID   GATB_AJECG              Reviewed;         564 AA.
AC   C0NV09;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial;
DE            Short=Glu-AdT subunit B;
DE            EC=6.3.5.-;
DE   Flags: Precursor;
GN   ORFNames=HCBG_06773;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in the
CC       mitochondria. The reaction takes place in the presence of glutamine and
CC       ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEH04822.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; GG663372; EEH04822.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C0NV09; -.
DR   SMR; C0NV09; -.
DR   STRING; 447093.C0NV09; -.
DR   EnsemblFungi; EEH04822; EEH04822; HCBG_06773.
DR   HOGENOM; CLU_019240_4_1_1; -.
DR   InParanoid; C0NV09; -.
DR   OrthoDB; 898782at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..88
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           89..564
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   mitochondrial"
FT                   /id="PRO_0000413238"
FT   REGION          26..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  62444 MW;  96C5CF1539B0B68F CRC64;
     MIRQCVSHRG IPCYRLAVRR VELTEPFHHP SPRPLGRKNW STSDEAKSKR AAMRKGGAPP
     PEHEDWELTV GIEIHAQLDT DAKLFSRASA ALDDVPNSNI ALFDIALPGS QPLFQPSTLI
     PAIRAAIALN CDIQRIRGQR IYELTHRLIE PYAKNGSIWL GAHDGIAKED GEGVQIGIKQ
     IQMEQDTAKS QELPSSTYLL DFNRVSRPLI EIITLPQIHS ATTAAACVRK IQAILQSVGA
     VTTGMEMGGL RADVNVSVRK RSEAAGDHQY DGVAGLGQRT EIKNLSSFKA VEYAIIAERD
     RQIAVLKAGG TIQGETRGWT LGSTETRKLR GKEGEVDYRY MPDPDLGPVI IGDDVISDLR
     RNIPVLPDEL LQMLVQDPKY GLSTVDAKTL IELDDGQRLE YYQDAVEILI TLQPDLSADF
     SAGKVVGNWV LHELGGLLTK SSAHWDSQRV PAQSLAEIIN LLSRKNITSS SAKSLLAMAF
     DGDKRSISQI VEDKNLLFQS LSRHEYIALA EEVMRQNPKM VSEIREKGQL GKMGWFVGQI
     KRIGDPNRVE AQKAEEILRE LILK