ID A0A1V6Q2R0_9EURO Unreviewed; 371 AA.
AC A0A1V6Q2R0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Alpha 1,4-glycosyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENANT_c016G09386 {ECO:0000313|EMBL:OQD83539.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83539.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000256|ARBA:ARBA00009003}.
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:OQD83539.1}.
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; MDYN01000016; OQD83539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q2R0; -.
DR OrthoDB; 5491454at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR Gene3D; 3.90.550.20; -; 1.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039367; Och1-like.
DR PANTHER; PTHR31834; INITIATION-SPECIFIC ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR31834:SF8; TRANSFERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14040)-RELATED; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..371
FT /note="Alpha 1,4-glycosyltransferase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013342775"
FT REGION 335..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 41055 MW; 30D8D2E3D43C3DFB CRC64;
MGRFHYLIGL LLLFLASSLW IALKLRDDTS SFPLGYSSCV CSEDVKMSEP SVELTPTVLP
QQSATSTHSE ATSLPEKLSY LPIKNSHGHQ KHSAFPAKLW QKSGPMGVSP ERQVEISSWL
EKNPALRHEI LTDGSADEYV REQFADYPQI LDLYLSLQVP ILKADLLRQL ILYADGGIWS
DLDVTCHEPI NTWIPKDFIS KSNVVVGLEF DGIQFSSWTV MTKPRTSHIV AVINYVTKAL
EDSATQHNVT MANLTMEMIS DVVDVTGPQA MTRALFQNLE LEMGLPMGRD NITNITQPTL
FQDVLVLPDA AFAAGQGGWP KNRGPYLVEH HYAGSWKNKD GGEQTNATKQ ADANQQADGN
QQADAKKPSD S
//