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Database: UniProt
Entry: A0A1L9SDG9_9EURO
LinkDB: A0A1L9SDG9_9EURO
Original site: A0A1L9SDG9_9EURO 
ID   A0A1L9SDG9_9EURO        Unreviewed;       473 AA.
AC   A0A1L9SDG9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPZODRAFT_99124 {ECO:0000313|EMBL:OJJ45246.1};
OS   Penicilliopsis zonata CBS 506.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX   NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ45246.1, ECO:0000313|Proteomes:UP000184188};
RN   [1] {ECO:0000313|Proteomes:UP000184188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KV878345; OJJ45246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9SDG9; -.
DR   STRING; 1073090.A0A1L9SDG9; -.
DR   VEuPathDB; FungiDB:ASPZODRAFT_99124; -.
DR   OrthoDB; 1694520at2759; -.
DR   Proteomes; UP000184188; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   CDD; cd06423; CESA_like; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   Pfam; PF13641; Glyco_tranf_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184188};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        54..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        432..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   473 AA;  54473 MW;  981FE7F0F1800D96 CRC64;
     MMFAWAVHYT SGAIQEWTPF LLVASYFVFS TCVYMLADTF ILGVFWFIYL VTNTYIAATT
     VLEAFLSLTA VHDSRKAVEK LAAKEWTFPT PDADLPVFDL IIVAYLPNEQ DIILSRIHYL
     LHQIVYPADK LRVNVIYNTP VPIEPVEQTM ADLAAKHDNL RVIKVPCSTS KADNINYYCR
     QVETEADVTA IFDCDHYPHP YGPRWAIERL MDRKVDIVQG RCIILNANEN LLTATIALEF
     DKIYAVSHPG RASMFGFGLF CGSNGYWRTS LLKRLQMDDS MLTEDIDSAL RAFGDGANAV
     HELNAISYEL APVSVSAFWK QRLRWAQGWL QASIRHVRLV WERAPPKPRS LKQRFGILSL
     LVIREWSYYL LTQYLCLVLS IIFKSFPVTG EEWLRILFFQ YPVAWWLFFF SVISLLATLY
     ITVAVRSEFV QWWMMGVFVC SYPLQLVLMA VIGLFGHARE VAKYVKWNPT PRN
//
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