GenomeNet

Database: UniProt
Entry: A1D6S8
LinkDB: A1D6S8
Original site: A1D6S8 
ID   GATB_NEOFI              Reviewed;         601 AA.
AC   A1D6S8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-APR-2013, entry version 41.
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=NFIA_065860;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL
OS   181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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
CC       glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase
CC       (AdT) complex, composed of A, B and C subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DS027690; EAW21422.1; -; Genomic_DNA.
DR   RefSeq; XP_001263319.1; XM_001263318.1.
DR   ProteinModelPortal; A1D6S8; -.
DR   STRING; 36630.CADNFIAP00005676; -.
DR   EnsemblFungi; CADNFIAT00005833; CADNFIAP00005676; CADNFIAG00005833.
DR   GeneID; 4589934; -.
DR   KEGG; nfi:NFIA_065860; -.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OrthoDB; EOG473T0X; -.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:HAMAP.
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:HAMAP.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:HAMAP.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:HAMAP.
DR   HAMAP; MF_00121; GatB; 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_amidoTrfrase-rel.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
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; SSF89095; GatB_Yqey; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Transit peptide.
FT   TRANSIT       1     52       Mitochondrion (Potential).
FT   CHAIN        53    601       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit B, mitochondrial.
FT                                /FTId=PRO_0000413264.
SQ   SEQUENCE   601 AA;  66768 MW;  70C56FC754772496 CRC64;
     MLQQWLRQSP GAARFLRGSC CRGPQSGSLR HSPLPTAPHR CIRSLQTSAT ESKEHIPLRK
     QLKQNAKALK AQKRQKRESE EASRQKWELT VGIEIHAQLN TETKLFSRAS TSNTDTPNSN
     VALFDLAFPG SQPEFQATTL LPALRAAIAL NCDIQPVSRF DRKHYFYHDQ PAGYQITQYY
     APFAKNGYVD LFPHDGIAPE DGDHVRIGIK QIQLEQDTAK SQEYPPSTQL LDFNRVSHPL
     IEIITMPQIH NPATAAACVR KIQAILQSCS AVTTGMELGG LRADVNVSIR RRDEAPGTHQ
     YGGIGGLGQR TEIKNLSSFK AVEDAVIAEK NRQIAVLESG GVIEGETRGW TIGSTETRKL
     RGKEGEVDYR YMPDPDLPPL IISHDLVSGL RDSLPTPPDQ LIEMLAGPEY GLSIEDAKPL
     IELDDGARLE YYQDVVDILR DLQQDQDAKS RAGLARMAGN WVLHELGGLC AKADLAWDAQ
     RVPAETLAQI IDQLQRKRIT GATAKQVLAM VFDGDRRPVP QLLEAENLLL RPLSRDEYIA
     LAEAAISQNP QMVEQIRAKN QLGKLGWFVG QMMRMGEKGR VEAQKADEIL RELILGKSDQ
     P
//
DBGET integrated database retrieval system