ID A0A1V6QUW8_9EURO Unreviewed; 748 AA.
AC A0A1V6QUW8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c035G11625 {ECO:0000313|EMBL:OQD93020.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD93020.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD93020.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYO01000035; OQD93020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QUW8; -.
DR STRING; 60172.A0A1V6QUW8; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000191612; 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:UP000191612};
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 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 84161 MW; 753E3E7AA50775D1 CRC64;
MDRRYGPDDQ DEKVELNTYR SGLHSNNSFE HPEPFSPSPV SPRPLTPIRP GHFPTDEYGQ
PVWLQPTARM SGHSDWDSRT PYDSRSASPT LYQNNGVQES HQSLAPLVTS PAPPAFEKDW
VKSGSIARIH DRDDAETWKG WKRWVFFLVP FLTLANTGIY LFYLGLRIFC IIMAQRIAHV
SYAGAWVFVA IEITVAIPSL MHNCWTMMAL KKRGRAKLRL TGNECPTVDV FITCCGEDDD
VVIDTVRGAC DQDYPRDQMR IIILDDAKSA SLEAACNELA VNHPNVIYMA REKIPGKPHH
FKAGNLNYGL DQVNLLPGGA GQFMAALDAD MIPEQDWLRA ILPHLLVDPK MALACPPQLF
YNTPASDPLA QSLDFFVHVI EPIKDALGVA WCTGSGYVVR REALEEIGNF PLGSLAEDVA
TSTLMLGRGW RTAYIHEALQ FGTVPEDFGG HLKQRTRWAI GTVDTAAKLK FCLWGDAVRE
MTFAQRFSGF LYATLSVYTL LLTLSLFAIP IILLWGKRLV AFATEEQLRW LIWSCFAATI
SNRLCEMALF IPAGYHTGQR GSRYQLWMSP YIALCIVRSF FLPTWLGGQT QAFKPTGSLG
SALNERDPKR SKNMFVRLRV ILLNYMASFH VAFVYVTLVG VVISSYRCFA QNSGFRDIII
CLITHAFWPP LTFLFICTSL WTPVSYAIDP PRMPEREELL TRDPKTGVAH PTKKSKKIAF
GGQAAWFELE YTVATVATIL VFIYSFMF
//
