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Database: UniProt
Entry: F1A2R6_DICPU
LinkDB: F1A2R6_DICPU
Original site: F1A2R6_DICPU 
ID   F1A2R6_DICPU            Unreviewed;      1205 AA.
AC   F1A2R6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Glucosylceramidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DICPUDRAFT_158887 {ECO:0000313|EMBL:EGC29519.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29519.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
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DR   EMBL; GL871422; EGC29519.1; -; Genomic_DNA.
DR   RefSeq; XP_003293963.1; XM_003293915.1.
DR   AlphaFoldDB; F1A2R6; -.
DR   STRING; 5786.F1A2R6; -.
DR   EnsemblProtists; EGC29519; EGC29519; DICPUDRAFT_158887.
DR   GeneID; 10505272; -.
DR   KEGG; dpp:DICPUDRAFT_158887; -.
DR   eggNOG; KOG2119; Eukaryota.
DR   InParanoid; F1A2R6; -.
DR   OMA; SEVWIGT; -.
DR   OrthoDB; 997839at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR006775; GH116_catalytic.
DR   InterPro; IPR024462; GH116_N.
DR   PANTHER; PTHR12654; BILE ACID BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR12654:SF0; NON-LYSOSOMAL GLUCOSYLCERAMIDASE; 1.
DR   Pfam; PF04685; DUF608; 1.
DR   Pfam; PF12215; Glyco_hydr_116N; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT   DOMAIN          388..738
FT                   /note="Glycosyl-hydrolase family 116 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12215"
FT   DOMAIN          808..1170
FT                   /note="Glycosyl-hydrolase family 116 catalytic region"
FT                   /evidence="ECO:0000259|Pfam:PF04685"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1205 AA;  136812 MW;  C19B0C7E04EDA2DD CRC64;
     MDDLFNFKSE ERDSNSGFDD VYEDINIGLE ASSPMSKQQQ QQQTSNNNGF LFNNIDDEDE
     ENFFVSPKQQ TSNLNSFSTT TNNSHHNSTS HYSFNNKISD EINLHFNFDD YDNSTTAINS
     SILNNNNNSN SNNSSSFFNK IIFNESTELF KSNSLIDDNN SNSSNNNINS NNNSNNNINN
     NINNELNSNI ISTMPGDNSF IYDNSNNNTS ITTNSYIEKL NTNNDNEITS PIEKGHVRNA
     SEQFSSPIQQ SQKKEEQEEN KKEDGKSSIF NLNSIKKAIL NTSNSNLLNF STDAFWKDLG
     DNPLIDQDTA SDQEKWLRLG EDIPQCSWAR RLDHNFPDHK HFQVSMWQGL KLVGIGYRMW
     KYVKKENSSG RVPMMDPFNL PKPGPIMGVP IGGIGSGSIN RGWRGDFVRW NMNSGLVTNE
     TVDVDKFSVY INFDDSNSAS SSTGSTPSGT FTPNGPNFDP SSTKSKQKAT VLYPGKPKNN
     LNLDVWNWGL KGENSCYFGL FPRAWTVYEE PHPDIKLVCK QISPVIPHNY QESSYPVGVY
     VWKIENNNKN SSADVSLMLT WQNSIGTKSD QDGGHYNKYF TLGDEPNKKI KGVTLIHRKE
     QRCAYNSSNI VYHDPMEYSI AVKDDPDVNI TFNERFETTS RLDAANLWYT FNKKGELENI
     QDSRPSAPKK PIGAAVAAKV KVPAGGSKTI VFCIAWDQPI TRFQLGSAYY KRYTKFYGNK
     GGNSQRIAYD ALQNYKSWDN QIAQWQNPII QDAELPSFYK MALFNELYYL VDGGTVWTHG
     SPQDQLPARY PLKTQLKPED ISDPNHIGRF AYLESLEYLM YNTYDVHFYS SYALAMLWPL
     LEISLQYDIA EATMLDYGIT WEGIHSGQQI PRKKRCTVPH DLGNPGEDPW KRVNSYNIQD
     ISRWKDLPSK FVLQVYRDYL VVEDKNFLLQ VYNVVEEVIQ RTLESFDTDH DGVVDNEGFP
     DQTYDVWPAV GCSAYSGGLW LASLKVASEM AKILGFKEDE SIYNAIFEKG SASYTKKLWN
     GYYFKYDCSN SVHADSIMSD MLAGHWYLLS CGLPSYMTFD QALSSLSIIN EYNVNSYGKE
     RCGAVNGMRP EGVVDNTCLQ SSEVWIGTSF SLAATMIQHH MDKDAWELVK GIVNSSYNRW
     GFQYQTPEAW DSNGCYRAGA YMRPLSIWSI QWALLKKKYF DFYDESLKSN NNSNNNINNG
     GSLLG
//
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