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Database: UniProt
Entry: A0A094DLS2_9PEZI
LinkDB: A0A094DLS2_9PEZI
Original site: A0A094DLS2_9PEZI 
ID   A0A094DLS2_9PEZI        Unreviewed;      1118 AA.
AC   A0A094DLS2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY60390.1};
GN   ORFNames=V497_03679 {ECO:0000313|EMBL:KFY60390.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY60390.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY60390.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY60390.1}.
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DR   EMBL; JPJZ01000808; KFY60390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DLS2; -.
DR   STRING; 1420910.A0A094DLS2; -.
DR   HOGENOM; CLU_000537_1_0_1; -.
DR   OrthoDB; 76239at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48050:SF13; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF06722; EryCIII-like_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   SMART; SM00726; UIM; 4.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          166..224
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          494..585
FT                   /note="Erythromycin biosynthesis protein CIII-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06722"
FT   REGION          28..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..981
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1083
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  119450 MW;  6EAE81DF1B482217 CRC64;
     MEPGTQDSGD SLPAAIIAQA EAACVGNADE IRSTQQRQSS ITSRPRQSAS GGAHGARGAS
     SSADRTSQPG NSDILGADGA VDPPPKYSEL EISQDGLDTK ARVTDDGRVN ITINQKTRRL
     SELLNPALRN QLSLVAQEDD QPLPPGYIPP SLGGQPGQIP PPSLNVVILV VGSRGDVQPF
     VALGKVLKSA YGHRVRLATH PVFQQLVEEN DLEFFSIGGD PAELMAFMVK NPGLMPGMDA
     LKSGDVGKRR KGMEEIVLGC WRACIEAGNG LGPAPKLEGG INMDTNPTER PFIADAIIAN
     PPSFAHVHIA EKLGIPLHMM FTMPWSPTQS FPHPLANIQS SNADVNMTNF ISYALVEMMT
     WQGLGDLINR FRERTLGLEP ISVIWGPGVL SRLKIPYTYC WSPALIPKPK DWGRHISVSG
     FFFLSLASSY QPEPELAEFL AAGPPPVYIG FGSIVVDDPN SMTSMIFEAV KKAGVRALVS
     KGWGGLGDDS LDPPEGVFML GNVPHDWLFK HVSCVVHHGG AGTSAAGIAL GRPTVVVPFF
     GDQPWWGAMI HRAGAGPEPI PYKDLTADKL AAAITEALKP STLEKAEELG VSISQEKGSE
     VGGKSFHDHL DWNSLRCSLA PNRVAVWQVK KTQVRLSALA ATVLANEGLL NFSDLKLYRP
     REYDTDDGPW DPISGGASAL FGTIASLSMG VADFPVELIK AFKPKPTSSA TDKTEALDED
     DVPSTTDNGT KPSQDSASKS QSQLSPSSTS QDGPSEQASS ATASRSSSKS ADQSSEPSSS
     TKQGKKQFDP SAITMESAIG ASKGISRVVG AGMKSPMDFT LGLARGFHNA PKLYGDDTVR
     PQERVTDFQS GLRAAGKGFG YGFYDGISGL VTQPMRGAEK EGAAGFIKGI GRGIGGIVFK
     PGAAIWGLPG YTMMGLHKEV RKMFGASVQA YIISARTAQG YEQWRTSTKE EQQYITSRWK
     GIKSKPGDIP AKPRHDSGKG KSDSNLGSAG AQQAPSANLD EDEEALRRAI EASIAHAAGS
     NTDDVSEADQ RAALEAAIQR SLADPEGSSS STHANEQDAE EAEQLKRAIE ESMRYHDRDV
     SATKTDEDIV MEYIKKQSLA EEEHRQSMLN STRSEDKK
//
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