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Database: UniProt
Entry: A0A194VA93_9PEZI
LinkDB: A0A194VA93_9PEZI
Original site: A0A194VA93_9PEZI 
ID   A0A194VA93_9PEZI        Unreviewed;       472 AA.
AC   A0A194VA93;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   SubName: Full=Initiation-specific alpha-1,6-mannosyltransferase {ECO:0000313|EMBL:KUI60942.1};
GN   ORFNames=VP1G_08155 {ECO:0000313|EMBL:KUI60942.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60942.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009003}.
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DR   EMBL; KN714763; KUI60942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VA93; -.
DR   STRING; 694573.A0A194VA93; -.
DR   OrthoDB; 5491454at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000313|EMBL:KUI60942.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW   Transferase {ECO:0000313|EMBL:KUI60942.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          404..431
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        436..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53574 MW;  20BB46CF30286048 CRC64;
     MRSPASSLSS MSPRSSLGPW SPTVPSLSSK FRNRVPTQMR RCIPIYLAFL IFFLIIANAD
     LFAVSVPRGS NQVFKRATDK KHKSNPTVPT IPLEGFPKKI WQTWKTDPLQ FEERDSSTAR
     TWVEKNPNFR YEVLTDSNDV GYVEQHFGPG GFDRPEIVEM YRNINATIIK ADLLRYMVLY
     AEGGVYADID VEALKPVSRF IPDHRYAEGD IDMVIGVEID QPQFKDHPIL GKKSQSFCQW
     TFMARPKLPV MLRLIEHIMG WLAGLAQQQN VPVSEVVLDF DQVISGTGPS AFTAAIIEEM
     NANRPKGTPE ITWDVFHDLD ESKIVSRVLV LDVEAFAAGQ GHSDSGNHNA RGALVKHHYH
     ASNWPSRHPR FNHPAYGSVE QCNWEPSCVA KWDADTAAFS LLSEEEQTKL VEDLRAEAQA
     QQAQQEQFLQ RIAQQDQLQQ QQQQQQIQNE PQHPLQPGQP LQQQEHEHEP HV
//
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