ID A0A1Q8S4X3_9PEZI Unreviewed; 483 AA.
AC A0A1Q8S4X3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=CCHL11_00908 {ECO:0000313|EMBL:OLN96426.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN96426.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN96426.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN96426.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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:OLN96426.1}.
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; MPGH01000017; OLN96426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8S4X3; -.
DR STRING; 708187.A0A1Q8S4X3; -.
DR OrthoDB; 2783297at2759; -.
DR Proteomes; UP000186583; 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; IPR008147; Gln_synt_N.
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:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000186583}.
FT DOMAIN 21..114
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 122..483
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 483 AA; 53602 MW; 0EFC4253D2088485 CRC64;
MAPSNDSITV ESLPELLKND NKVKLAGIDV DGMLRGKLVS KNKFLSIAKS GFGFCSVIFG
WDMHDMTYAK ELKISNAENG YHDLIAIPDL SSFRRIPWED NVPFFLVSFH DPDTQEPICA
CPRGLLKNAL DKLKAQGYGA MAGAEYEFYQ FKTPVRSSET SSSTAGYLQE NPPQALPSLT
EGMFGYSLTR TVHNKDYFYD VFETCAQFSC DIEGWHTESG PGVFEAALEF GEIQQMADRA
SLFKYVVKSV ATKYGITPCF MAKPKHGLPG NSGHMHVSIV DKDGKNLFAR ETKDENPPYP
DVAGLSDLGR HFLAGLLDGL PDIMPLLAPT INSYKRLVEN FWAPVTVSWG LEHRAASIRL
IAPPTSKPGA TRFEVRVPGA DTNPHFVLAA ILALGWRGVE KKLEIPVPPL GKGEDVGGKS
DKGVRLAKSL REANDRFTRK ESIAREVFGD DFVDHFGGTR DHEIRLWEEA VTDWEVKRYI
ETV
//
