GUX1A_NEUCR
ID GUX1A_NEUCR Reviewed; 521 AA.
AC Q7SA23;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
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; ORFNames=NCU07340;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002239; EAA33262.1; -; Genomic_DNA.
DR RefSeq; XP_962498.1; XM_957405.2.
DR AlphaFoldDB; Q7SA23; -.
DR SMR; Q7SA23; -.
DR STRING; 5141.EFNCRP00000007117; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR EnsemblFungi; EAA33262; EAA33262; NCU07340.
DR GeneID; 3878646; -.
DR KEGG; ncr:NCU07340; -.
DR VEuPathDB; FungiDB:NCU07340; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR InParanoid; Q7SA23; -.
DR OMA; VYSNIKV; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..521
FT /note="Exoglucanase 1"
FT /id="PRO_0000270622"
FT DOMAIN 485..521
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..450
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 447..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..485
FT /note="Linker"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 493..510
FT /evidence="ECO:0000250"
FT DISULFID 504..520
FT /evidence="ECO:0000250"
SQ SEQUENCE 521 AA; 54741 MW; 230B7A488120B272 CRC64;
MLAKFAALAA LVASANAQAV CSLTAETHPS LNWSKCTSSG CTNVAGSITV DANWRWTHIT
SGSTNCYSGN EWDTSLCSTN TDCATKCCVD GAEYSSTYGI QTSGNSLSLQ FVTKGSYSTN
IGSRTYLMNG ADAYQGFELL GNEFTFDVDV SGTGCGLNGA LYFVSMDLDG GKAKYTNNKA
GAKYGTGYCD AQCPRDLKYI NGIANVEGWT PSTNDANAGI GDHGTCCSEM DIWEANKVST
AFTPHPCTTI EQHMCEGDSC GGTYSDDRYG GTCDADGCDF NSYRMGNTTF YGEGKTVDTS
SKFTVVTQFI KDSAGDLAEI KRFYVQNGKV IENSQSNVDG VSGNSITQSF CNAQKTAFGD
IDDFNKKGGL KQMGKALAKP MVLVMSIWDD HAANMLWLDS TYPVEGGPGA YRGECPTTSG
VPAEVEANAP NSKVIFSNIK FGPIGSTFSG GSSGTPPSNP SSSVKPVTST AKPSSTSTAS
NPSGTGAAHW AQCGGIGFSG PTTCQSPYTC QKINDYYSQC V
