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Database: UniProt
Entry: A0A165DCR4_EXIGL
LinkDB: A0A165DCR4_EXIGL
Original site: A0A165DCR4_EXIGL 
ID   A0A165DCR4_EXIGL        Unreviewed;       476 AA.
AC   A0A165DCR4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glutamine synthetase/guanido kinase {ECO:0000313|EMBL:KZV84241.1};
GN   ORFNames=EXIGLDRAFT_294881 {ECO:0000313|EMBL:KZV84241.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV84241.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV84241.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV84241.1,
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}.
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DR   EMBL; KV426233; KZV84241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DCR4; -.
DR   STRING; 1314781.A0A165DCR4; -.
DR   InParanoid; A0A165DCR4; -.
DR   OrthoDB; 2783297at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
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:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 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   Kinase {ECO:0000313|EMBL:KZV84241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Transferase {ECO:0000313|EMBL:KZV84241.1}.
FT   DOMAIN          121..476
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   476 AA;  52923 MW;  8C8155FE6B62C6DB CRC64;
     MAVSPKNLDE LKTLLANDNK VKVAGIDVDG VLRGKFMSRD KFLSAAKDDG FGFCSVIFGW
     DMHDTVYPKE LLISNRQNGY RDLLARIDLS LMRRIPWEDN VPLFLLSFCD PETKEPVSVC
     PRGALKKAMK IAEEKGWRCM AGCEYEYFQF KETPYTAAEK GFTRLTPLTP GMHGYSMLRT
     TLNQDYFHDL FNMSEQFGIS IEGHHTETGP GVFETALTYT DALRMADNAI LFKLLAKSVG
     IKHGIMPSFM AKPWGNLPGC SGHTHVSLRT ADGKNLFAVA DGKPRSDAQY EDTRFISQEA
     EWFLAGVLEG LADIVPLLVP TINGYKRLVG GESFWAPNAV TYGYDSRAAS VRIISPPSCP
     PASTRFEVRV PGADMLPHYA IAAIFLTGLR GIAKRLPLPC EPIATLQARP GGKESVVKLA
     KSLEDATREM MKKGSVAREV FGDEFVEHYG GTRLHEVDLW NEAVTSWEVE RYLELA
//
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