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Database: UniProt
Entry: A0A1Y2GDI4_9FUNG
LinkDB: A0A1Y2GDI4_9FUNG
Original site: A0A1Y2GDI4_9FUNG 
ID   A0A1Y2GDI4_9FUNG        Unreviewed;       999 AA.
AC   A0A1Y2GDI4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Oxysterol-binding protein-domain-containing protein {ECO:0000313|EMBL:ORZ06103.1};
GN   ORFNames=BCR41DRAFT_425225 {ECO:0000313|EMBL:ORZ06103.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ06103.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ06103.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ06103.1,
RC   ECO:0000313|Proteomes:UP000193648};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC       {ECO:0000256|ARBA:ARBA00008842}.
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:ORZ06103.1}.
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DR   EMBL; MCFF01000047; ORZ06103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GDI4; -.
DR   STRING; 64571.A0A1Y2GDI4; -.
DR   InParanoid; A0A1Y2GDI4; -.
DR   OrthoDB; 960at2759; -.
DR   Proteomes; UP000193648; Unassembled WGS sequence.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.160.120; -; 1.
DR   Gene3D; 3.30.70.3490; -; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR037239; OSBP_sf.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041680; PH_8.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR10972:SF216; OXYSTEROL-BINDING PROTEIN HOMOLOG 3; 1.
DR   PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF15409; PH_8; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193648};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..216
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   DOMAIN          228..319
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          52..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..583
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   999 AA;  112583 MW;  0BE54FEFC8E389E5 CRC64;
     MQEIEVPPRD VFQHYVHIDQ ADKTLVWWFS TKRKNISFGL FFRKSAPPQL KSNTLAPSIT
     SINTSPPRAE SVHSKQHSQH SPGGSYNGHY TKDGILSTSP TKSCRASNYA SSRASIDTTS
     DDEESTELAD GLGTNQQNPS QSSLPPGSQP SVRRKKTVAK FKDPELIEIM PIQHYESSSG
     TIRGEFTVKE EGSYVLVFDN SFSINTSKRL TFFVALEERS RKPVAQPTSE MSGWMLKKKR
     KRMQGWAKRW FQIDNGVLSY YKAPDSPCRG KVHLVLSTVT VSQASNMIHI DSGTMLYHLK
     ALSVEDYNAW ISVMKAIKNS DKAAHDTVHR MIQRESSVKR AQLRNSWIGS NNELDQLKEI
     MSSMDAGFLD IKEQLESIRP HTETPPPNSG SSQKSTRERQ MSVDSNNSNP NNSNNPNNNN
     NKFKISKFGF SSGLQRTTSD GSLASTQSSI ESIHAKLLAS FAKLSSDKEK AFEIMRSEIQ
     KWEKNEKHFR LLLTENENLS TTRTGEKSSL ARHALEEAYI ARNSMASERT HSFTSSIHTG
     SDDIFYDADD TVLTADLSSA DLSDLEGAGF DDHDDDNDNS SDDESAEEPA KEPQPEEVKA
     PQPTVSSNDP LSEGPIVRRS VLPAPVSGED ISLLSILRKN VGKDLSTVAM PVSLNEPINV
     LQRLCEELEY SELLDKAAGL SDSLDRLVYV SAFAVSGYAT TQWRAARKPF NPLHGETFEY
     VCPEKGFKFI SEKVSHYPPI MACHADSVNG WTLAMDSRAK TKFWGKSMEL MPNGTIHIHF
     QKTGDHFTIH KPSTWMRNLM AGTKYLEHTG DLKVVNHATR ETCVLTFKES SFFAGTKNEV
     VGSVMDASGA KKRSLQGKWN ESLMEELGPN KFERLWKVNN PPPNHEKYYG FTEFTIHLNE
     MTKGLEAKLP KTDTRFRPDQ SLFERGLVEE ADKEKLRVEQ KQRDLRKTME ANGEPWVVRW
     FEKRPDPQTD DPEGQTWHYK GGYWETRETG QWNEPVTLW
//
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