ID A0A0D2ILT0_9EURO Unreviewed; 779 AA.
AC A0A0D2ILT0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_06029 {ECO:0000313|EMBL:KIX97951.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX97951.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX97951.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX97951.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KN848072; KIX97951.1; -; Genomic_DNA.
DR RefSeq; XP_016632074.1; XM_016776532.1.
DR AlphaFoldDB; A0A0D2ILT0; -.
DR STRING; 1442371.A0A0D2ILT0; -.
DR GeneID; 27711775; -.
DR VEuPathDB; FungiDB:Z520_06029; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000053411; 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; cd06421; CESA_CelA_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:UP000053411};
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 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88168 MW; BAD73265D73925AA CRC64;
MPPLRKADRR RFEQPPMTEM STVSMQSTLR QSQESFIEKP TTVHPVYGSY RESVSLDEQP
RLARRPGLSD LHNRTLSDLM TESIADSSLE PPNGGFPPFA PGAGSGAVST YSESQTRSSS
PYPVPSPFRS QETLKPLVPD APSTFFKRDW IREGSIAQLH SRDDKEFLSG KKRLLFRWVA
PLLCLISLSL YWFYFGLRIA FIIDAQHHYK APFPLAWVFV AIEISIAVPI FMQTLWSLFI
LKKRHRPKLR LVGNEVPTVD VFITCCGEDD DLILDTVRAA CDLDYPQDRY RVILLDDGKS
DPLKNVLEEM RETFPNVFYM RRPKFPGVPH HFKAGNLNYG LDAVQSLPGG SSEFMAALDA
DMIPEQQWLR AVLPHLLIDE KMGLACPPQL FYNVPRDDPL CQSLDFFVHV SEPVKDALGV
AWCTGSGYVA RTVALAQIGN FPCGSLAEDV ATSTLLLGSG WKTAFVHEAL QFGTVPEDYG
GHLKQRTRWA IGTVDTAFKL KFCLWGDKVR QMTFAQRSSS FIYAFLSLFN IFLTLSIFAM
PIVLIANKPL VAYANDTQLR WLIRACFANM VFNRLCEFVL FIPAGYATGQ RGSRYQLWMA
PYISLTIIRS FILPTWLGGQ RQAFKATGSI KSALNERDPK LRAPMWRRIW TICVNYLAGF
HVAYVYFVLV AVTLSSYRTF LTQHTLRGKL IGLLTHAFWP PLAWLIVCSS FWIPFTYACD
PPNCPDREEL LVRDPKTNVA HPTAEAKKVA FAPQTVLFEL EYTFTTAFTA LVFVAAFFY
//
