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Database: UniProt
Entry: B8PML2_POSPM
LinkDB: B8PML2_POSPM
Original site: B8PML2_POSPM 
ID   B8PML2_POSPM            Unreviewed;       806 AA.
AC   B8PML2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Glycoside hydrolase family 5 protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=POSPLDRAFT_134779 {ECO:0000313|EMBL:EED77883.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED77883.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; EQ966506; EED77883.1; -; Genomic_DNA.
DR   RefSeq; XP_002476919.1; XM_002476874.1.
DR   AlphaFoldDB; B8PML2; -.
DR   KEGG; ppl:POSPLDRAFT_134779; -.
DR   HOGENOM; CLU_009024_1_0_1; -.
DR   InParanoid; B8PML2; -.
DR   OMA; NEFIPPW; -.
DR   OrthoDB; 69117at2759; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31308; -; 1.
DR   PANTHER; PTHR31308:SF1; PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        782..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..325
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          655..763
FT                   /note="Glycoside hydrolase family 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18564"
SQ   SEQUENCE   806 AA;  90205 MW;  44E9B0BAEA65F61A CRC64;
     MISRTASDAS FIFVRQDQDA SQDLAASRLT ESELLVDKSN VETPRAEVDR ALAQPQSPAA
     RPPAPKAAPS FAHDWSAAGT GGRLYTHGRH FVDAYGRVCN LRGVNLAGNC KTPTNHDHDT
     FPANHADVTF VGRPFPLEEA HEHFARLRRW GLTFIRFLVT WEAVEHAGPG IYDTEYLAYL
     RSILSLLPQF GLTAFVALHQ DVWSRYTGGS GAPAWTLEAV GFDLHGLEEP GAAWLRGVRG
     GGHTEDERGL WPCGYQKLSA ATMATCFWAG DAFAPKLRVR DARGADVSIQ TFLQTAFLDM
     WEVVAKTVGD LEGVLGFEIM NEPHRGYAEL QSMHQFDYNT DLHLGHVPTA FQSFTLGAGY
     PTEVGFWTRT FPMPTRLTGK AVLNTARQKA WRQDGPTGGR CLWEMHGVWG WDLKKNEGVV
     LRESYFKKHP MTGKTIDWYT DFFYPFVQRW AERVRSVSSP DKLVLVEPIP NEFCPSSWTP
     ERQPPNVVYA PHWYDLNALF TKAFGDFTAN VQGLSRGMFI LKALYWGHQG ARENFSLQIR
     NIVEAGYRSL GERPVVIGEC GIPMDMNKGE AFQTDSWIWQ TRMMDAMLTA LDKSLVGFTL
     WNYNPDNEDH IGDDWNGENF SWFSRRRALT GDWLDLAQTS PTLDNGARIV RAFVRPYPAK
     TAGIPVRFDY EMNTGQFTFE WVIPGVDSAP PAEASVASPP LASHPALTSK DTQIFLPSLL
     AHSRKIVVQG LKPEDRYRYD EARQTLTITT ADLVPGERHS VTVSLNPPLK DAFTVNSFWD
     DFGLHVVAAT IVLASILIYV IMSMVS
//
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