ID A0A1Y2WJ55_9PEZI Unreviewed; 492 AA.
AC A0A1Y2WJ55;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Glycosyltransferase family 62 protein {ECO:0000313|EMBL:OTB08888.1};
GN ORFNames=M426DRAFT_316914 {ECO:0000313|EMBL:OTB08888.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB08888.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB08888.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB08888.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family.
CC {ECO:0000256|ARBA:ARBA00037964}.
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DR EMBL; KZ111525; OTB08888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WJ55; -.
DR STRING; 1001833.A0A1Y2WJ55; -.
DR InParanoid; A0A1Y2WJ55; -.
DR OrthoDB; 2965755at2759; -.
DR Proteomes; UP000242955; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43083; MANNAN POLYMERASE II; 1.
DR PANTHER; PTHR43083:SF2; MANNAN POLYMERASE II COMPLEX ANP1 SUBUNIT; 1.
DR Pfam; PF03452; Anp1; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW Transferase {ECO:0000313|EMBL:OTB08888.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 56261 MW; CB924CCD93373FC2 CRC64;
MMSRHHSAGF SNGYPRNNNN NNNSTFDISP HRFQPRASTP ASRRRRSLLT RLGILAIVVI
LIWLFIWPGS GSFTSIFSLG LISASGDVLM DTVRYYDLSN VQGTARGWER EERILMCVPL
RDAEQHLPMM FSHLRNFTYP HHLVDLAFLV SDSKDRTLEM LVENLEGLQA AEDPKLPYGE
ISIIEKDFGQ KVNQDVESRH GFAAQASRRK LMAQARNWLL SATLRPYHSW VYWRDVDVET
APFTILEDLM RHNKDVIVPN VWRPLPDWLG GEQPYDLNSW QESETALALA DTLDEDAVIV
EGYAEYATWR PHLAYLRDPY GDPDMEMEID GVGGVSILAK ARVFRSGVHF PAFSFEKHAE
TEGFGKMAKR MQFSVVGLPH YTIWHLYEPS VDDIRHMEEM EAERQAKEAE EKEKQDREKK
VKEQFGDANA QWEQDKSEIQ NLAKEAAQKE QDSESRQDSG SESKVESGQD SQKAVFEKVG
EKPQDNQARV AA
//
