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Database: UniProt
Entry: A0A317WAR1_9EURO
LinkDB: A0A317WAR1_9EURO
Original site: A0A317WAR1_9EURO 
ID   A0A317WAR1_9EURO        Unreviewed;       497 AA.
AC   A0A317WAR1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Nucleotide-diphospho-sugar transferase {ECO:0000313|EMBL:PWY82985.1};
GN   ORFNames=BO70DRAFT_33301 {ECO:0000313|EMBL:PWY82985.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY82985.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY82985.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY82985.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
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:PWY82985.1}.
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DR   EMBL; MSFL01000011; PWY82985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WAR1; -.
DR   STRING; 1448321.A0A317WAR1; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_33301; -.
DR   OrthoDB; 1985716at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31646:SF5; (MNN2), PUTATIVE (AFU_ORTHOLOGUE AFUA_6G04450)-RELATED; 1.
DR   PANTHER; PTHR31646; ALPHA-1,2-MANNOSYLTRANSFERASE MNN2; 1.
DR   Pfam; PF11051; Mannosyl_trans3; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:PWY82985.1}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..497
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016338841"
FT   REGION          38..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  56134 MW;  F4F1943478AB7F5C CRC64;
     MFPARTFLRA RTLVLALILV FAFTWSYAHW QDFPFPEQDH PAQSETGTVS DKKQTGKWRH
     NPEGHIEFWR KFQPLLTTHQ PKCEPPLRLG SAPSIRFEQS NPEDRPELLD MLPFDVDAMR
     NAHSGFVDAI NAHPPQLNYT PNTRGLVSTA GGSYLPVLVI SLRMLRRTGS KLPVEVFLAN
     DDEYEDHICD VVLPSLNARC VVMSEILDAV SGTMEIQKYQ FKLFAMLFSS FEEILFLDAD
     AFPLQQPELL FTSEPFASTH MVTWPDFWAS TISSYYYEIS SQPYPETAVR QSSESGEVLI
     SKKTHLKTLL LSTYYNVWGP DFYYPLLSQG AAGEGDKETF IAAASRLQES YYQVSEPICA
     IGHGTEGGLA GSAMVQFDPM QDFALTRKGE WRVHGSTAPA PRAFFVHANY PKFNPATVFE
     KQAVNPAYAD DGSYTRAWTI PEDVIKAFGS DVEKGFWEEI LWTACELEDK FGTWKDERGV
     CLGVKNYWNA MFGIGHS
//
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