ID W9RGH1_9ROSA Unreviewed; 834 AA.
AC W9RGH1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Protein fluG {ECO:0000313|EMBL:EXB75910.1};
GN ORFNames=L484_022587 {ECO:0000313|EMBL:EXB75910.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB75910.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; KE344693; EXB75910.1; -; Genomic_DNA.
DR RefSeq; XP_010098822.1; XM_010100520.1.
DR AlphaFoldDB; W9RGH1; -.
DR STRING; 981085.W9RGH1; -.
DR eggNOG; KOG0683; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase 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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR Pfam; PF04909; Amidohydro_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 SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030645}.
FT DOMAIN 502..834
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 834 AA; 93022 MW; E766EA6155BE96AC CRC64;
MDFSELRETI EEAELVDAHA HNIVAANSTF PFINGFSEAH GDALSLAPHS LSFKRNLKDI
SELYGCEKSL SGVEEFRRVH GLQLISLTCF KATKISAILI DDGLTLDKMH DIEWHKAFAP
FVGRILRIER LAETILDKEF PGRSSWTLDT FTANFITVVG EIFGLKSIAA YRSGLEINTN
VSRREAEEGL AEVLQAAKPV RITNKNFIDY IFTRSLEVAQ QFDLPMQIHT GFGDKDLDMR
LSNPLHLRTV LEDKRFLECR IVLLHASYPF SREASYLASV YSQVYLDIGL AVPKLSVHGM
ISSVKELLEL APTKKVMFST DGYAFPETFY LGAKKAREVI FSVLRDACVD GDLTLHEAVE
AAKDIFSENA VRFYKIKLPV KSFGSTNSIS PIPAKIKITA QSDVSLVRVL WVDASGQHRC
RVVPAARFQD VVEKNGVGLT FATMGMTSFT DGPADETNLT GTGEIRLMPD LLTRRRIPWQ
TREDMVLADM HLRPGEPWEY CPREALRRVS KLLKEEFDLV MNAGFENEFF LLKSVLREGK
EEWMPFDSTP YSSTSAYDAA SPIFQEVVST MHSLNIPVEQ LHAEAGKGQF ELALGHATCT
HAADNLIFTR EVIRAIARKH GLLATFMPKY SLEDIGSGSH VHLSLWQDGK NVFMGSSRHG
MSKVGEEFMA GVLHHLPAIL AFTAPLPNSY DRIQPNTWSG AYQCWGKENR EAPLRTACPP
GISDGYVSNF EIKSFDGCAN PHLGLAAVLA AGIDGLRRHL TLPEPVDANP SSLDAELQRL
PRSLSESLGA LKEDAVITEL IGKKLLVAIK GIRKAEIDYY LKHKDAYKQL IHRY
//