ID   GUX1B_NEUCR             Reviewed;         516 AA.
AC   P38676;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   22-FEB-2023, entry version 105.
DE   RecName: Full=Exoglucanase 1;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase 1;
DE   AltName: Full=Exocellobiohydrolase 1;
DE   Flags: Precursor;
GN   Name=cbh-1;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=7642129; DOI=10.1016/0378-1119(95)00288-h;
RA   Taleb F., Radford A.;
RT   "The cellulase complex of Neurospora crassa: cbh-1 cloning, sequencing and
RT   homologies.";
RL   Gene 161:137-138(1995).
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This protein, although sequenced from the genome of strain 74-
CC       OR23-1A, has only limited sequence identity to the corresponding
CC       protein produced by the locus NCU07340 determined in the complete
CC       genome sequence of Neurospora crassa 74-OR23-1A, due to extensive
CC       nucleotide sequence discrepancies mostly in the N-terminus.
CC       {ECO:0000305}.
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DR   EMBL; X77778; CAA54815.1; -; Genomic_DNA.
DR   PIR; S42093; S42093.
DR   AlphaFoldDB; P38676; -.
DR   SMR; P38676; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GlyCosmos; P38676; 2 sites, No reported glycans.
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:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..516
FT                   /note="Exoglucanase 1"
FT                   /id="PRO_0000007922"
FT   DOMAIN          480..516
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          18..445
FT                   /note="Catalytic"
FT   REGION          444..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..480
FT                   /note="Linker"
FT   ACT_SITE        223
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        488..505
FT                   /evidence="ECO:0000250"
FT   DISULFID        499..515
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  54472 MW;  38E598406EA81900 CRC64;
     MRASLLAFSL AAAVAGGQQA GTLTAKRHPS LTWQKCTRGG CPTLNTTMVL DANWRWTHAT
     SGSTKCYTGN KWQATLCPDG KSCAANCALD GADYTGTYGI TGSGWSLTLQ FVTDNVGARA
     YLMADDTQYQ MLELLNQELW FDVDMSNIPC GLNGALYLSA MDADGGMRKY PTNKAGAKYA
     TGYCDAQCPR DLKYINGIAN VEGWTPSTND ANGIGDHGSC CSEMDIWEAN KVSTAFTPHP
     CTTIEQHMCE GDSCGGTYSD DRYGVLCDAD GCDFNSYRMG NTTFYGEGKT VDTSSKFTVV
     TQFIKDSAGD LAEIKAFYVQ NGKVIENSQS NVDGVSGNSI TQSFCKSQKT AFGDIDDFNK
     KGGLKQMGKA LAQAMVLVMS IWDDHAANML WLDSTYPVPK VPGAYRGSGP TTSGVPAEVD
     ANAPNSKVAF SNIKFGHLGI SPFSGGSSGT PPSNPSSSAS PTSSTAKPSS TSTASNPSGT
     GAAHWAQCGG IGFSGPTTCP EPYTCAKDHD IYSQCV
//