ID A0A081CFP6_PSEA2 Unreviewed; 655 AA.
AC A0A081CFP6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glycosyl hydrolases family 32 superfamily protein {ECO:0000313|EMBL:GAK65492.1};
DE SubName: Full=Related to Sucrose-6-phosphate hydrolase {ECO:0000313|EMBL:SPO46500.1};
GN ORFNames=PAN0_009c3709 {ECO:0000313|EMBL:GAK65492.1}, PSANT_04186
GN {ECO:0000313|EMBL:SPO46500.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK65492.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK65492.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK65492.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO46500.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO46500.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR EMBL; DF830076; GAK65492.1; -; Genomic_DNA.
DR EMBL; OOIQ01000010; SPO46500.1; -; Genomic_DNA.
DR RefSeq; XP_014656155.1; XM_014800669.1.
DR AlphaFoldDB; A0A081CFP6; -.
DR SMR; A0A081CFP6; -.
DR GeneID; 26304513; -.
DR HOGENOM; CLU_013784_3_0_1; -.
DR OrthoDB; 2298551at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18621; GH32_XdINV-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42800; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR PANTHER; PTHR42800:SF3; GLYCOSYL HYDROLASES FAMILY 32 SUPERFAMILY; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758}.
FT DOMAIN 120..471
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 510..647
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 71080 MW; C09497D640C32EC3 CRC64;
MSPVPTSTSV LPPQAAVEAR TSVADAESSQ SFQKRTMRPA QLPLPQQNGQ LLQDSHPSAS
SEDSSSSSPT LFPVTTPASS GVPSPTDEVK QADMLTPHAA LENATRSTKA LFEQWRPTSH
FLGPHGWMND PCGPSYDPRT RLYHLWYQWN PNASTWGSIC WGHAYSHDMI HWTSRPYPVI
EPGSNHDSEG VFTGCVLHRS PLGSAAEAAE TGEMTAIYTA VSKLPIHHTL PYNHGSEKVV
LSTSKDGGET WVPHGLVLDG PPEHLDVISW RDPYIAPWPL LDAALGRTDQ QPGLYALIAG
GIKDTTPTIF AYSINPTDLS QWTFVGTLAD VGRNHKAAPY GVDLGKNWEV ANFFTIRDTA
GPASAEYLLI NVEGCTEPGP ARAAVYMETL PDVQRGSDGE IRLQPDHVGL LDHGCLYAAS
SFHDEQHDRR IMWGWITEDD LPEDYYNTQG WAGLISLPRE LFHHPTSTQL GIRPAQEVQR
LRNGAQHICI TPSDRAATAV VELAEVDSLG AILVDEVASR SYEVETKLSA GQPGVVVAHS
NDMTTRTVVY ITDSELVVDR SLSAGKDAVI AKGLKVNTST LRAPLAPTAD GTHSLRLFLD
NSVLEVFVDD VIALSTRVYP DPTDVGLSIL QTSDAQQADL APVNVWQGLS KALIA
//
