ID   A0A2V5IFL0_9EURO        Unreviewed;       503 AA.
AC   A0A2V5IFL0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Alpha-1,2-mannosyltransferase {ECO:0000313|EMBL:PYI27310.1};
GN   ORFNames=BP00DRAFT_439307 {ECO:0000313|EMBL:PYI27310.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27310.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI27310.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27310.1,
RC   ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ825573; PYI27310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5IFL0; -.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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   Glycosyltransferase {ECO:0000313|EMBL:PYI27310.1};
KW   Transferase {ECO:0000313|EMBL:PYI27310.1}.
FT   REGION          377..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  57435 MW;  631F12F58C55D16B CRC64;
     MFPSRAALRI RIRIILAGLF LVLICGQSFS RWRKQTAPSQ AQLTWRHATE GHIEFWRQFQ
     PLLTTYEPKC LPPLRLGMAP SIRFEQADPY DQTEFLDLLP MDIEDLQQTH RGFLNAIKTT
     PPQLNYTRNT RGLVSTAGGS YLPVLVLSLR MLRRTGSQLP VEVFLASEDE YETYICDVVL
     PSLNAQCIVL STILSAIPHS IHIEKYQFKL FAMLFSSFEE ILFLDADAFT LFPPETLFTQ
     DPFLSHGLIT WPDFWASTIS PSYYEITGQP APKPPTRPSS ESGEVLLSKR SHQRTLLLST
     YYNIHGPEFY YPLLSQGAAG EGDKETFVAA ATALAEPHYQ VAEPLCAIGH TTQRGGFAGS
     AMVQFDPTED FARHRHREET RKPQPQAHGF FLSPPNTTRT APRTPRAFFI HANYPKFDPA
     TVFDAHEVNP AIGDDGRYTR AWTGPPEIIR AFGRDVEKEF WEEIRWTACE LEGRFRAWEG
     KKGVCKRVEK YYRAMYGGRW WGW
//