ID A0A150FVA1_GONPE Unreviewed; 563 AA.
AC A0A150FVA1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=GPECTOR_403g238 {ECO:0000313|EMBL:KXZ41542.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ41542.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|ARBA:ARBA00007072}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ41542.1}.
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; LSYV01000400; KXZ41542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150FVA1; -.
DR STRING; 33097.A0A150FVA1; -.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 19..272
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 201..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 60672 MW; 7DF9A84B5B3DCB56 CRC64;
MGLGGWQVPE GNTTVLSRTY TDDKTWAAAW MCWSEKLARG VVTGPLCTAA RDRGAEMLEV
LREGHVSTDN MFAPALLLLR QLGVGGTSYV ARWIAGLTLS FLDPWVSQPK PPCDLCSPKE
MCVTEGGLVI KEAGAGVLQY TAGMAFVAVA AGRPGAPGSS AIPLQTQRDW TCWAKGQLDS
MVGAKTGQAF VTGLDTVLPS DSEITVPKSP RHKGSACGGG PGCAAPSQAN RRQLVGALLG
GPNRDDSYTD DRNAPGTGPT TSIEHNAGFT AAVMKRTGIM YGSPNAPAVH VTCSPPRTDI
LYLPRGHILI SGSNTTDRLV GVDRQTPYSL VMQDNGNLAL LWGPSIFGVV AFNFTGQRYV
TYVMWETGTV ADRSRGPFKL SWIEPNGGLT VTDAAGVSLW EYWLPDMGDI TPAGLELWFS
NGYPPYWTSR FVDRDFNVPQ ICQFLSIQRL QRGALDYAGS RRSYGSEGFP VTHLTSGTTL
PAANSTSPRD RLVVFTRDFE LILHPDGNLE FIRQRYQYNG TWGISLRQSG SNKLTTPDMA
PFMLTFIEPS GQLAVLDKTG AAI
//
