ID A1C6U9_ASPCL Unreviewed; 511 AA.
AC A1C6U9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Cellulose hydrolase, putative {ECO:0000313|EMBL:EAW14120.1};
GN ORFNames=ACLA_071530 {ECO:0000313|EMBL:EAW14120.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14120.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14120.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382}.
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DR EMBL; DS027045; EAW14120.1; -; Genomic_DNA.
DR RefSeq; XP_001275546.1; XM_001275545.1.
DR AlphaFoldDB; A1C6U9; -.
DR STRING; 344612.A1C6U9; -.
DR EnsemblFungi; EAW14120; EAW14120; ACLA_071530.
DR GeneID; 4708062; -.
DR KEGG; act:ACLA_071530; -.
DR VEuPathDB; FungiDB:ACLA_071530; -.
DR eggNOG; KOG2566; Eukaryota.
DR HOGENOM; CLU_031530_1_0_1; -.
DR OMA; SKRFWAF; -.
DR OrthoDB; 1844890at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR049161; GH59_cat.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR Pfam; PF02057; Glyco_hydro_59; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAW14120.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..511
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633320"
FT DOMAIN 475..511
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 454..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 54061 MW; 12D8E33849F28DE1 CRC64;
MTLLILLAGL ATAASALTAT VNTAQTYQTM DGFGFSQAFG RAYDLYNIPS DQRDYALDLL
FSPTKGAGMT ILRNRIGSSS GDSILPNSPG SPNSIPHYKA LGTDSVQVWV TQQAVKYGVK
TIYADAWSAP AFMKTNGEEK SGGYLCGVTG KTCPSGDWKQ AYANYLVQYI KDYAELGLDI
SHVGFLNEPD YTVSYSSMLS DGTQAADFIK VLHPTLQKAG LSHVGITCCD ATGWSAQKTR
TAELIAANAE GLLSRITSHS YSSDPTSPMG ANIPVWQTET ADLSGAWETT WHSSGGKGEG
LTWAEKIHTA ITQGGVSAYL YWEGFERATT NACLVITDGK RVIPSGRLWA FGHWSRYVRP
GAVRVAISGS TSTLKMTAFK NKDGTVSVQI INTGPSASEV TVAGFAAASA KAYLTDNNHA
QISETTVSVN GGKASVNVPG HAFVTVVLSG NGSRVPPSLS PATKPETKPE TGNAVVTGRW
SQCGGQGWTG PTACAAPYTC KAQNPWYSQC L
//
