ID A0A0D1ZGF8_9EURO Unreviewed; 769 AA.
AC A0A0D1ZGF8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_06744 {ECO:0000313|EMBL:KIW26961.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW26961.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW26961.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW26961.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847043; KIW26961.1; -; Genomic_DNA.
DR RefSeq; XP_016247177.1; XM_016393758.1.
DR AlphaFoldDB; A0A0D1ZGF8; -.
DR GeneID; 27345938; -.
DR VEuPathDB; FungiDB:PV07_06744; -.
DR HOGENOM; CLU_016061_0_1_1; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000054466; 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:UP000054466};
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 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..128
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 16..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 87242 MW; 2BC9153179D8BC6F CRC64;
MPPLRKSDRR RSDQPPMTEM STVSMQSTLR QSQESFIEKP TTVHPVYGSY RESESLDQPR
LSRRPGLSDL HNRTLSDLMT ESIADSSLEP PNGGFPPFAP GAGSTYSESQ TRSSSPYPRS
QETLKPLVPD NPSTYFKKDW VKEGSIAQLH SRDDKEFLSG KKRWLFRWVA PLLCLISLSL
YWFYFGLRIA FIIDAQHHYK APFPLAWVFV AIEISIAVPI FMQTLWSLFI LKKRHRPKLR
LVGNDVPTVD VFITCCGEDD DLVLDTVRAA CDLDYPQDRY RVLLLDDGKS DALKNVLEEM
RETFPNVYYI RRPKFPGVPH HFKAGNLNYG LDAVHSLPGG ASEFMAALDA DMIPEQQWLR
AVLPHLLMDE KMGLACPPQL FYNVPKDDPL CQSLDFFVHV SEPVKDALGV AWCTGSGYVA
RTVALAQIGN FPCGSLAEDV ATSTLLLGSG WKTAFVHEAL QFGTVPEDYG GHLKQRTRWA
IGTVDTAFKL RFCLWGDKVR HMTFAQRSSS FIYAFLSLFN IFLTLSIFAM PIVLIANKPL
VAYANDTQLR WLIRACFANM VFNRLCEFVL FIPAGYATGQ RGSRYQLWMA PYISLTIIRS
FVLPTWLGGQ RQAFKATGSI QSALNERDPK RRAPMWRRIW TICVNYMAGF HVAYVYFVLV
AVTLSSYRTF LTQHTLRGKL VGLLTHAFWP PLAWLIVCSS FWIPFTYACD PPNCPDREEL
LVRDPKTNVA HPTPEAKKIA FAPQSVFFEL EYSVTTAFTA LVFVAAFFY
//
