ID   B6QSS8_TALMQ            Unreviewed;       803 AA.
AC   B6QSS8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Glycosyl transferase, putative {ECO:0000313|EMBL:EEA19402.1};
GN   ORFNames=PMAA_001970 {ECO:0000313|EMBL:EEA19402.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA19402.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; DS995905; EEA19402.1; -; Genomic_DNA.
DR   RefSeq; XP_002152339.1; XM_002152303.1.
DR   AlphaFoldDB; B6QSS8; -.
DR   VEuPathDB; FungiDB:PMAA_001970; -.
DR   HOGENOM; CLU_016061_0_1_1; -.
DR   OrthoDB; 352133at2759; -.
DR   PhylomeDB; B6QSS8; -.
DR   Proteomes; UP000001294; 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:UP000001294};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEA19402.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        196..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        541..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        679..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        713..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        785..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  90158 MW;  7A484292B83B9262 CRC64;
     MSGYHNGHYG GTTSPYGNGN NGNPNAYYGN NTYGYGEEMV EFDVLNHGHG QNDAAYMNSV
     NMNDHYDPNE RHIGRSPPKP IRPGLQPADD FASPMGSPLG TPGGQMGWPL PTRRGHDRHV
     DSFASVSSTP AGSRSATPAF IRQYQNNQSF QSHQSLAALV DQPPSPLYSK DWVQQGSIAR
     VADRDDVDIW KGWRRYVYML VPFLTFGNTA IYIFYLGLRI TCVILAQNAA NQTYAGAWVF
     IALELATAIP SMMHNAWTMW ALKGRQRPKL RLTGDDCPNV DVFITCCGED DEVVIDTVHA
     AADQDYPLDK FRVIVLDDAK SSSLEASVRQ LALTYPNVHY MARTKIPGVP HHFKAGNLNY
     GLEQTRLMPG GAGQFMAALD ADMIPEQQWL RATLPHLLID PKMALVCPPQ LFYNCPPADP
     LAQSLDFFVH VIEPIKDALG VAWCTGSGYV VRREALDDIG QFPLGSLAED VATSTLMLGK
     GWRTAYIHEA LQYGTVPEDY GGHLKQRTRW AIGTVDTAFK LKFCLWGDAI KEMSFAQRFS
     GFLYATLSLY TILLTASLFA IPIILIWGRP LVAYATNEQL KYLIWACFAS TMSNRLCEFA
     LFIPAGYHTG QRGSRYGMWM SPYLALCIIR SFFLPKWLGG QTQAFKPTGS LGSALEERDP
     KRRKGMVRRL WTILVNYMAM FHFAFVYLTI VAVCLSSYRC FFQNDPNNFK NVFLCLITHA
     FWPPVTFLFV ITSLWTPIAY AIDPPSMPDR EDLLKRDPKT GVAHPTPESK KIAFAGQEAW
     FEFEYTFATL FTIFVFVYSF FYI
//