ID A0A2V5HXK5_9EURO Unreviewed; 560 AA.
AC A0A2V5HXK5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Putative alpha-1,3-mannosyltransferase {ECO:0000313|EMBL:PYI29219.1};
GN ORFNames=BP00DRAFT_448660 {ECO:0000313|EMBL:PYI29219.1};
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:PYI29219.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI29219.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI29219.1,
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; KZ825535; PYI29219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HXK5; -.
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; PTHR31392; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR PANTHER; PTHR31392:SF1; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:PYI29219.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PYI29219.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..560
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016172284"
SQ SEQUENCE 560 AA; 61690 MW; E6540B3D3EA9326E CRC64;
MLSRALLLVF LVLYCFKATL LTIEYHHAGL CAPPLYKRED PTAAIADTHS QSPLALANPP
PSSNTLPSFD RTNFTKSLSH LLSLLPDSSQ AQDLTSPITS TGEAKLHELG LRTRVFRSLF
AAWEAVHLVP TATGPLTRDD ILQVLQTDPS IAHDLQTDTS TLMHSYETLR TFYTQLSTRL
FDWTTPYFPS HATLHTQFHN GGRGLVLTAG DKQAPYVLTS LQSLRQQGCT LPVEIMYLGD
DDLSEDARDA LEAIPDVITR DLSPMVSDAG WTLRGWAAKP FAILLSSFRE AIFIDADALF
LTNPADLFHD PGYVQTGALF FKDRLLMPGE KRAWLRQVLP APLSRAVHRS RMWTGQSIHM
QESGVVVVDK WRHFVALLLV TRLNGPDRDG DKALGKVGVY DMVYGDKETF WLGWELVGDP
DYAFHEGAAA VMGTAQVNRA RGTGNETAEE ADAGSGNPED PRFRICAPQL LHLGTDGRPL
WFNGWLLPNK YSDDPRQQPA AFEAFITEPP DATAVGAWKL QQNNVCCLAA DQVGRFSAAE
KAVLEGVVQL AKEVGAIGEE
//