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Database: UniProt
Entry: A0A0D0B4L0_9AGAR
LinkDB: A0A0D0B4L0_9AGAR
Original site: A0A0D0B4L0_9AGAR 
ID   A0A0D0B4L0_9AGAR        Unreviewed;       439 AA.
AC   A0A0D0B4L0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   SubName: Full=Unplaced genomic scaffold GYMLUscaffold_38, whole genome shotgun sequence {ECO:0000313|EMBL:KIK58245.1};
GN   ORFNames=GYMLUDRAFT_45464 {ECO:0000313|EMBL:KIK58245.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK58245.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK58245.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK58245.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN834786; KIK58245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0B4L0; -.
DR   HOGENOM; CLU_009600_0_0_1; -.
DR   OrthoDB; 2105587at2759; -.
DR   Proteomes; UP000053593; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT   DOMAIN          29..420
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          130..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  47582 MW;  C1046CFCDD69AB59 CRC64;
     MSTHDLHRLT ASEALQLIRT DQISVEEYAR SLLKRVESRD SQVQAWAYLN PNLILSQARA
     LDKVPKEERG PLHGIAIGVK DIMYTKDMPT EHNSPLYKGS LIQVDASPVM TLRNSGALIF
     GKTTTTEFAS TTVGPQTSNP YNKGRTPGGS SSGSGAAVAD MQVPIALGTQ TGGSIIRPGS
     FNGILGYKPT WGAISREGVR MYSINLDTVG FYARSVQDLQ LLADVFRLQD DEIPKPFILP
     GATFALCKTE VWPEAGPGTI KAMERAAELL RAAGAETVEL DLPEDFNGMQ DLHRRISQGD
     GRAAFLGEYT TAKDKLDTFL VGQVENVSGI TRREYLEALD VVASLRPKID RIASRYAAIL
     TPSVPDEAPE GIESTGSAVF NAMWTALHIP VVNIPGFSGS SKLPIGLSLV APRYKDRYLL
     NVSEEISKVF GNGGWQSDL
//
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