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Database: UniProt
Entry: A0A2H3IKM2_9EURO
LinkDB: A0A2H3IKM2_9EURO
Original site: A0A2H3IKM2_9EURO 
ID   A0A2H3IKM2_9EURO        Unreviewed;       474 AA.
AC   A0A2H3IKM2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glycoside hydrolase, family 30 {ECO:0000313|EMBL:PCH05305.1};
GN   ORFNames=PENO1_023000 {ECO:0000313|EMBL:PCH05305.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH05305.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH05305.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH05305.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC       {ECO:0000256|ARBA:ARBA00005382}.
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:PCH05305.1}.
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DR   EMBL; NPFK01000042; PCH05305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IKM2; -.
DR   SMR; A0A2H3IKM2; -.
DR   STRING; 290292.A0A2H3IKM2; -.
DR   OrthoDB; 1844890at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR039514; 6GAL-like.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR   PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR   Pfam; PF14587; Glyco_hydr_30_2; 1.
DR   Pfam; PF17189; Glyco_hydro_30C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PCH05305.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..474
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013769860"
FT   DOMAIN          23..240
FT                   /note="Endo-beta-1,6-galactanase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14587"
FT   DOMAIN          380..469
FT                   /note="Glycosyl hydrolase family 30 beta sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17189"
SQ   SEQUENCE   474 AA;  51540 MW;  27C37C67E93E1345 CRC64;
     MVFSKVAVAA SALSLGAYAI DAQINVDLQA RYQSVDGFGC SQAFQRAEDI FGKYGLSPKN
     QSYVLDLMYS EERGAGFTIL RNGIGSSNSS TSNLMNSIEP FSPGSPSSTP NYTWDHYNSG
     QFPLSQQARA RGLPYIYADA WSAPGYMKTN QDENWSGFLC GIEGETCPSG DWRQAYADYL
     VQYVKFYAES GVPVTHLGFL NEPQEVVSYA SMGSNGTQAA EFVKILGQTL EREGIDIELT
     CCDGVGWSEQ EAMIPGLQVV GPDGKSAEDY LSVVTGHGYS SAPTFPLSTK RRTWLTEWTD
     LSGAFTPYTF FADGGAGEGM TWANHIQTAF VNANVSAFIY WIGAENSTTN SGMINLINDE
     VIPSKRFWSM ASFSKFVRPN AQRVKATSSD ASVTVSAFEN TNGVVAIQVI NNGTSAASLT
     IDLGKTHKEV KKVVPWVTSN DYDLEEMSEI DVKHNSFLAS VPARSLTSFV TECE
//
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