ID   A5E3B6_LODEL            Unreviewed;       933 AA.
AC   A5E3B6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Glycosyl hydrolase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LELG_04103 {ECO:0000313|EMBL:EDK45924.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK45924.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK45924.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; CH981528; EDK45924.1; -; Genomic_DNA.
DR   RefSeq; XP_001525071.1; XM_001525021.1.
DR   AlphaFoldDB; A5E3B6; -.
DR   STRING; 379508.A5E3B6; -.
DR   GeneID; 5232001; -.
DR   KEGG; lel:LELG_04103; -.
DR   VEuPathDB; FungiDB:LELG_04103; -.
DR   eggNOG; ENOG502QPU8; Eukaryota.
DR   HOGENOM; CLU_009024_0_1_1; -.
DR   InParanoid; A5E3B6; -.
DR   OMA; MWQTFLT; -.
DR   OrthoDB; 69117at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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:SF5; ERGOSTERYL-BETA-GLUCOSIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT   DOMAIN          126..317
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          795..874
FT                   /note="Glycoside hydrolase family 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18564"
FT   REGION          685..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..716
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  106463 MW;  6F1CF6A9A5ED3BB3 CRC64;
     MKSARYAHDA ITDRLKLYLT TTSIITTPNL KSLRRRYPPT QNIPKADNDT GSIIPCTRLT
     TDGKGDFYDE ATGRKIHLKG INVDSQMKLP VEPYMPSYLG NCRDPHNIFF EGDTVSFVGR
     PFPLEDAPSH FQRIKSWGYN TIRYLLTWEA IEHEGPGKYD QSFADYTVQM LRIIGEIGGL
     YVFLEFHQDV WSRFSGGSGA PMWTFYAAGL EPKNFAETEA AILHNDPRFH DDSEIYHKML
     WTSNYKRLAS LVMFTLFYGG KNYFPDLMMN GENIQDYLQG KYLGSVDFIW KNICDNCGDL
     IDNGTILGFE SMNEPNGGLI GHPRLDVLPA NQQLRVGTTP TVFQTFMLGM GLTCEIDEYQ
     ISITGPRKSG TKIVDPKGVR AWVSPEIGAK LDLHYGFKRS ENWVLGTCPF AEMGIWKWPP
     ALLTTDLSEL TQSQRLEITS KSILIDPDYY NKVLPQQNYE EKSHQGKIFA KIDSEVFINY
     HFVNHIIKFK QVIRKHAPDV FVLILTPVLE QPPDLAHDDR KIVDKKTVYC PHYYDGMSLM
     FKSWNSKYNV DTLGIMRGCY LNPVLGIVFG ERAIRNCIRK QFAEMRRECN TYLGPIPIVM
     SETGMPFDMD EKRSYRNGKH ISQTAALDAL CNALEGAHNL SHTFWCYNSM NNHKWGDNWN
     NEDFSFWSPE DRNLEFDDYY EEEKVDTDPI ENVTQRARKS SRTKRLKKKA RNATKMGRTS
     SRHSSVSTTN SDSPSFYEES DTETSNSTLT STAMGLSSSQ ASSIISLTSS NIKHRQLKNC
     YPSPDGVRAV NAVIRPYLMA SRGTIVESEF DFKSRKFSLQ LSVMKGAAEN RFKPSVIFVP
     KWHFPFLDYG DIYLTSGYIK YNEELEYLEW YHAPDPSIVQ EEEQEEEQEA TATMKRQGSP
     IFTTETIVIK NNSGSLDEVK LTGGKSELGC PIT
//