ID A0A094EHE0_9PEZI Unreviewed; 473 AA.
AC A0A094EHE0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN ORFNames=V499_02813 {ECO:0000313|EMBL:KFY77944.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY77944.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY77944.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY77944.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY77944.1}.
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DR EMBL; JPKB01000426; KFY77944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EHE0; -.
DR HOGENOM; CLU_042555_4_1_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01908; YafJ; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR026869; EgtC-like.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR PANTHER; PTHR43187:SF1; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR Pfam; PF13230; GATase_4; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962}.
FT DOMAIN 2..263
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 325..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52387 MW; B1F112D99310EAC7 CRC64;
MCRFLVYKGS DEILLSKLIL DPSHSILTQS FDSRLRLDTR RPHNGDGFGI GYYTDPKLGP
EPCIFTSTIP AWNCINLQRI ASKTASPLIF AHVRATTEGS LSDDNCHPFR HGSLMWMHNG
GLGAWKYIKR RLGERLADKW YLGVCGGTDS EWAFALYLDT LERMGHDPSN PPEHGFGPGI
LRQAMLKVIK DINQFIAEVP PKLIVEEKVD TRSLLNFAVT DGHSVICTRY VSSQTDEAAS
LYYSSGSTWH DEKKGNFQMD RRDKGADIVL VASEPLTFER DNWVTVPTNS TLTIHNQTVM
VHPIIDENYS QNPAHKRSAQ FVAEKGLTTN PTSKPCTETG TSTPSSVSTS KATSPSESYN
KHVSLPVSRL NECMSGLSVR SLSPESASDS GYRPVLSGRD PSRPQEQGNI KKKRVSLIEI
DPQVLRDADQ DYQSLGSQSQ RSGRLGSGNT SPNPDRTNYG SAAKITQYFP ELS
//