ID A0A165B525_EXIGL Unreviewed; 380 AA.
AC A0A165B525;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE SubName: Full=Arabinanase/levansucrase/invertase {ECO:0000313|EMBL:KZV79831.1};
GN ORFNames=EXIGLDRAFT_734182 {ECO:0000313|EMBL:KZV79831.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79831.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV79831.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79831.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KV426556; KZV79831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165B525; -.
DR InParanoid; A0A165B525; -.
DR OrthoDB; 2418563at2759; -.
DR Proteomes; UP000077266; 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; cd18820; GH43_LbAraf43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007855487"
FT REGION 32..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 41592 MW; AEB5008C11D8B1C9 CRC64;
MLLKFAVSLI LASSVLLSGV HAAAGTSCAV STTTTAPTTT SAPPKTTTSK STATPKPTNA
GLPPLPTFPK TFKNPIKPGT GADPWVIYSK KYDTYYLIQS AGGGLKVHSS RDLTTFGQNV
TKVWSTPKDM TGVWAPELDY IDNNWYIYVA IQTTKENASH RMFVLKGTSD DPQQPFKMVG
KITSPDDNWA IDGTVMQYKP NGALYFIWSG WKDTKSGNEQ NLYIAKMCGP TKICSDRVLL
HEPKQKWQRS GSSGVNEGPE ILVHGDRTFL VYSAAGSWTD NYCLALMGID GGKDPMSPKN
WWRLDDRPVM SSSDTALAPG HASFTTDRKG TPYVVYHAID HKGAGWSGRT IRTQSFKWNK
DGSPWFPQPV GFNTSLPHPA
//
