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Database: UniProt
Entry: A0A1V8SQ90_9PEZI
LinkDB: A0A1V8SQ90_9PEZI
Original site: A0A1V8SQ90_9PEZI 
ID   A0A1V8SQ90_9PEZI        Unreviewed;       597 AA.
AC   A0A1V8SQ90;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03147};
DE            Short=Glu-AdT subunit B {ECO:0000256|HAMAP-Rule:MF_03147};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03147};
GN   ORFNames=B0A48_13441 {ECO:0000313|EMBL:OQO01198.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO01198.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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).
CC       {ECO:0000256|HAMAP-Rule:MF_03147}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_03147};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_03147}.
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:OQO01198.1}.
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DR   EMBL; NAJO01000032; OQO01198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SQ90; -.
DR   STRING; 1507870.A0A1V8SQ90; -.
DR   InParanoid; A0A1V8SQ90; -.
DR   OrthoDB; 5474932at2759; -.
DR   Proteomes; UP000192596; 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   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; 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   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.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03147};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03147};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03147};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03147}; Reference proteome {ECO:0000313|Proteomes:UP000192596}.
FT   DOMAIN          433..595
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   597 AA;  65711 MW;  3816135F0F5137C5 CRC64;
     MSVPSVRLRS LKALPALYTR PGYTTRPCYV SKWLQSRGLQ VSTAPPPNAV PLRKHLKDEA
     KRKKADAKAG TGLRRDNAVT ARLQKWELTV GIEVHAELNS ACKLFSSATA ASGDSTAVPN
     SNVAAFDAAL PGAQPQFQVA TLLPALRAAV ALGCDIQRKS GWDRKHYFHW DQPNGYQITQ
     YYQPFAKDGA IRLSAEDGVP EEDLLGGRSL LIGIKQIQME QDTAKTTHHP PSSYHIDYNR
     SGHPLIEIIT LPHIHSPQTA AAVVRKLQSV LKAVDACTTG MELGGLRADV NVSVRQRGTI
     GSSSYSGVAG LGQRTEIKNL SSFKAVEDAI VAERDRQISV LEAGGIIAGE TRGWSLGSTE
     TTRLRGKEGE VDYRYMPDAD LPPLIIGNDL IDHLRDRLPE LPDTTVERVQ REYGVTEKDA
     RTIVALDDGD RLEYMEATVE LLQPRLLDVD DLKLGKLAGN WVLHELGGFL TANNLCWSDL
     KIYPIDLADI IAYLTRGEIT SRTAKQLLEY SNDDSTSRRV GDLIYDLGLL LRPLSDDEYT
     ELARTIMDEN PGMVAAVKEK GQKGKIMWFV GQMVRRGEEG TIEPGKAKEV VERMLAE
//
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