ID F8PRJ4_SERL3 Unreviewed; 748 AA.
AC F8PRJ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Glycoside hydrolase family 5 protein {ECO:0000313|EMBL:EGO01133.1};
GN ORFNames=SERLA73DRAFT_167273 {ECO:0000313|EMBL:EGO01133.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; GL945478; EGO01133.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PRJ4; -.
DR STRING; 936435.F8PRJ4; -.
DR eggNOG; ENOG502QPU8; Eukaryota.
DR HOGENOM; CLU_009024_1_0_1; -.
DR InParanoid; F8PRJ4; -.
DR OMA; NEFIPPW; -.
DR OrthoDB; 69117at2759; -.
DR Proteomes; UP000008063; 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; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR041036; GH5_C.
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; 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, ECO:0000313|EMBL:EGO01133.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 727..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 588..705
FT /note="Glycoside hydrolase family 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18564"
FT REGION 623..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 84506 MW; 9403B6E2C4769DF9 CRC64;
MSSFAHDWSA TGTGGKLKTH GRHFLDSYGR VCSLRGVNVS GSSKAPANHD NGTFPANHDT
VTFVGRPFPI KEAHEHFSRL RRWGLTFIRF LVTWEAVEHA GPGLYDHGYL TYIHELLSLL
PRYGMSAFIV VHQDVWSRYS GGSGAPAWTL ESIGFDLHAL EESGAAWLLG VKGGGHVEAE
RGIWPCGYQK LAAATMATCF WAGDTFAPKL KIQAPDGQLK SVQQYLQDAF LDMYTVVAQR
LGDLDGVLGF EIMNEPHRGY IDLPSLYAFD YNTDLHLSHV PSAFQSFMLG SGYPTEIGHW
TRSFPMPTRL TSNTVLNSAS RKAWRTDGPT QGKCVWEMHT VWGWDLDKNE GVVLRENYFV
KDPMTGRKVD WYTDFYYPFL RRWADRVRSV SPNDKILFVE PIPNEFCPSS WTPERQLPNM
VFSPHWYDLN ALFAKAFGDF TVNVQGLSRG MFPLKAFYWG QQGARDNFSL QLRNIVEAGY
KALGEKPVLI GECGIPMDMN HKEAFMDDDF KWQARMMDAM MTGLEQALVG FTLWNYNPDN
DDEKGDDWNG ENFSWFSRRR AMPPILLDFD QTSFTLDNGA RILPSVVRPY PAKTAGIPIG
FSYEMTTGVF TYEWAVPDTS DQNFSKGTKG NSQSNASVSR PPLSDHPAVN ARETEIYVPS
LLTHGRKLLV EGLEPEDKYF YDPARQTLYI VPHDFKPGKT HKVTVSIKPP PRPAFQVNSF
WSDFGEMFSS GSVVFLGILI FIYTRYNG
//