GH6D_PODAN
ID GH6D_PODAN Reviewed; 429 AA.
AC B2ADA5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable exoglucanase GH6D {ECO:0000305};
DE EC=3.2.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=GH6D {ECO:0000303|PubMed:23645193}; OrderedLocusNames=Pa_4_550;
GN ORFNames=PODANS_4_550;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [3]
RP IDENTIFICATION.
RX PubMed=23645193; DOI=10.1128/aem.00327-13;
RA Poidevin L., Feliu J., Doan A., Berrin J.G., Bey M., Coutinho P.M.,
RA Henrissat B., Record E., Heiss-Blanquet S.;
RT "Insights into exo- and endoglucanase activities of family 6 glycoside
RT hydrolases from Podospora anserina.";
RL Appl. Environ. Microbiol. 79:4220-4229(2013).
CC -!- FUNCTION: Probable exoglucanase that may play an important function in
CC biomass degradation by catalyzing the hydrolysis of cellulose.
CC {ECO:0000250|UniProtKB:B2ABX7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; CU633454; CAP61420.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP27774.1; -; Genomic_DNA.
DR RefSeq; XP_001903645.1; XM_001903610.1.
DR AlphaFoldDB; B2ADA5; -.
DR SMR; B2ADA5; -.
DR STRING; 5145.XP_001903645.1; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR PRIDE; B2ADA5; -.
DR EnsemblFungi; CAP61420; CAP61420; PODANS_4_550.
DR GeneID; 6187939; -.
DR KEGG; pan:PODANSg660; -.
DR VEuPathDB; FungiDB:PODANS_4_550; -.
DR eggNOG; ENOG502SATK; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 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..429
FT /note="Probable exoglucanase GH6D"
FT /id="PRO_5001338837"
FT DOMAIN 394..429
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 240..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 162
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 429 AA; 45612 MW; 8823BFCF9623318D CRC64;
MRAVYAILAG LLATGSASPL EARQSGNPFV GRSLFVNPKY SESLERTRQA FLSRGDQTNA
AKVQYVQNKV GTFVWISNIF LLRDIDDAIR NARAAQSRGE KPIVGLVLYN LPDRDCSAGH
SSGELSLDQN GLNRYRTEYV QPFAQKLKAA SDLQFAVILE PDAIGNMVTG TTAFCRNARG
PQQDGIAYAI QQLQASNIHL YLDVANGGWL GWADNLKPTT ILQKAGSNAR IRGYSSNVSN
YNPYSTNNPP PYTAGSPSAD ESRYATSLGN ALRERGLPTN FIIDQGRVAL DGARKEWGEW
CNVSPAGFGQ PFTTNTNNPN VDAILWVKPG GESDGTCGMS GAPQAGAWFD AYAQMLTTNA
HPEIRADGGG GGSPAPGPSS TAVAPSPSAT PGGNCAARWA QCGGQGWTGP TCCAQGTCQA
SNQWYSQCL
