ID A0A1X2IB48_9FUNG Unreviewed; 759 AA.
AC A0A1X2IB48;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=GS catalytic domain-containing protein {ECO:0000259|PROSITE:PS51987};
GN ORFNames=BCR42DRAFT_419212 {ECO:0000313|EMBL:ORZ13115.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ13115.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ13115.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ13115.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, 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:ORZ13115.1}.
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DR EMBL; MCGE01000017; ORZ13115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IB48; -.
DR STRING; 90262.A0A1X2IB48; -.
DR OrthoDB; 2783570at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 1.20.120.1560; -; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR040577; Gln-synt_C.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR022147; GSIII_N.
DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT DOMAIN 200..651
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 759 AA; 84561 MW; 26482A6FABB3E538 CRC64;
MAHEARVNSV VGSLAKAPRN VQFPTTKEGG GRLQSTSEIF GQNVFSLKEM SKMLPKPVYK
NFVKQLKGNE TLDKVTADAI AHAVKVWAIQ RNASHFTHWF QPLNDSTAEK HDSFLTMKSN
FVDGFEEVTA IDTFSGSQLL QSEPDASSFP SGGMRTTFEA RGYTVWDTKS PMFIQDGPHG
TSILYVPSVF ISYNGEALDE KSVLLRSAET LNKVAVEVLN MIEPKDEDKP RTKSVFATLG
TEQEYFLIDR ALYTLRPDLK ITGRTLLGGL PPRHQQLEDH YFGKIPTRVL AAISEAEYEL
ARLGVPIKTR HNEVAPAQFE VAPIFEEAML AVDHNMLTMD VLHRVAHRHK LKVLFHEKPF
RGVNGSGKHC NWSLSTDQGD NLLDPSSSPE TNLRFLFFLV ATLKAVYDHG DLLRAGIASA
SNDHRLGAHE APPGIISAFL GSQLNEVLNA VEEGRPVNYD ATGTQLQHVR ISGTVLDLKV
ATLPSIARDL TDRNRTSPFA FTGNKFEFRA VGSKQSVSFP VTLLNSAVAS SLMEMRDALA
KQKGAKEIAS KEDQLAVIRD FIKQSKPIRF EGDNYSDEWV QEAARRGLPN IVKSPDAFPR
LLRAENAAML RKTGVFSETE LQSRYHILVE KYCKDVMIEA QTLLTMVTQQ VMPAAFQYRR
DLAEAASYMS KVGVASGPEV NLLNQLTPVV ADLQAEIKTL RAMLDKMIHI EDLEVLAKES
SEYVLTSMNK VRNLADELEC HVADKLWPLP KYTELFLNI
//
