ID   CBHA_NEOFI              Reviewed;         452 AA.
AC   A1DMA5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Probable 1,4-beta-D-glucan cellobiohydrolase A;
DE            EC=3.2.1.91;
DE   AltName: Full=Beta-glucancellobiohydrolase A;
DE   AltName: Full=Cellobiohydrolase D;
DE   AltName: Full=Exocellobiohydrolase A;
DE   AltName: Full=Exoglucanase A;
DE   Flags: Precursor;
GN   Name=cbhA; Synonyms=celD; ORFNames=NFIA_052720;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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   -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; DS027698; EAW15926.1; -; Genomic_DNA.
DR   RefSeq; XP_001257823.1; XM_001257822.1.
DR   AlphaFoldDB; A1DMA5; -.
DR   SMR; A1DMA5; -.
DR   STRING; 36630.CADNFIAP00005098; -.
DR   EnsemblFungi; EAW15926; EAW15926; NFIA_052720.
DR   GeneID; 4584338; -.
DR   KEGG; nfi:NFIA_052720; -.
DR   VEuPathDB; FungiDB:NFIA_052720; -.
DR   eggNOG; ENOG502QPHV; Eukaryota.
DR   HOGENOM; CLU_020817_3_2_1; -.
DR   OMA; ALTWSKC; -.
DR   OrthoDB; 875234at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; PTHR33753; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..452
FT                   /note="Probable 1,4-beta-D-glucan cellobiohydrolase A"
FT                   /id="PRO_0000393545"
FT   REGION          406..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        226
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        231
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48193 MW;  51B9A887942F04DB CRC64;
     MHQRALLFSA LAVAANAQQV GTQKPETHPP LTWQKCTAAG SCSQQSGSVV IDANWRWLHS
     TKDTTNCYTG NTWNTELCPD NESCAQNCAV DGADYAGTYG VTTSGSELKL SFVTGANVGS
     RLYLMQDDET YQHFNLLNNE FTFDVDVSNL PCGLNGALYF VAMDADGGMS KYPSNKAGAK
     YGTGYCDSQC PRDLKFINGM ANVEGWKPSS NDKNAGVGGH GSCCPEMDIW EANSISTAVT
     PHPCDDVSQT MCSGDACGGT YSATRYAGTC DPDGCDFNPF RMGNESFYGP GKIVDTKSEM
     TVVTQFITAD GTDTGALSEI KRLYVQNGKV IANSVSNVAD VSGNSISSDF CTAQKKAFGD
     EDIFAKHGGL SGMGKALSEM VLIMSIWDDH HSSMMWLDST YPTDADPSKP GVARGTCEHG
     AGDPEKVESQ HPDASVTFSN IKFGPIGSTY KA