GenomeNet

Database: UniProt
Entry: A0A165FCT6_EXIGL
LinkDB: A0A165FCT6_EXIGL
Original site: A0A165FCT6_EXIGL 
ID   A0A165FCT6_EXIGL        Unreviewed;       458 AA.
AC   A0A165FCT6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=EXIGLDRAFT_650801 {ECO:0000313|EMBL:KZV88780.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88780.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV88780.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88780.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV426090; KZV88780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165FCT6; -.
DR   STRING; 1314781.A0A165FCT6; -.
DR   InParanoid; A0A165FCT6; -.
DR   OrthoDB; 2534858at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          121..458
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   458 AA;  49927 MW;  7C978DBB7C21F26B CRC64;
     MSSAEQYRAL SASLRANSVT YVRLAWVDLI GWTRYRVIPI AQFDKLLKSA RPGVRLTEAS
     LGLVFMQLAD GFHSSGEYLY VVDPSSMRLC NSYAAGHAIV MGWFERAIPS PNAPLSVPLC
     PRGQLRRIVT EAERTHGVKI RMGFEVEVIF LKSAVPLDAV NDFGWSLSKA IPSGSVIAQV
     LEEIANGLQH SGVELLMYHA EAAPGQYEFV TNHLPPLEAV DALIATKETI SNIASKYGLQ
     ATQAPRLYND TCGSGLHVHL SVSSSRASAS ANVPSAPGFS ALEASFLQGM LDHLPGVCAL
     SLPTDASYAR MLDGIWSGGT WASWGRENRE SAIRVCGEEG NYHFEVRAHD GTACSYIAMA
     ALIAGGMRGV RSSAPLVTKD CQKLASSLSG DERRELGISR RMPLKLEEAR QYLTQDQEMK
     ADLGEDFVKT FLAVNETLQS ALKDETEEKT IKKLVDHY
//
DBGET integrated database retrieval system