ID A0A1V6RWN1_9EURO Unreviewed; 592 AA.
AC A0A1V6RWN1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
DE AltName: Full=Endo-beta-1,4-mannanase F {ECO:0000256|ARBA:ARBA00033295};
GN ORFNames=PENVUL_c020G05346 {ECO:0000313|EMBL:OQE06046.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE06046.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans.
CC {ECO:0000256|ARBA:ARBA00002993}.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates.
CC {ECO:0000256|ARBA:ARBA00025192}.
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 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:OQE06046.1}.
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DR EMBL; MDYP01000020; OQE06046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RWN1; -.
DR STRING; 29845.A0A1V6RWN1; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 553..589
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 430..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 64173 MW; B1C9A4248E3D3CD1 CRC64;
MMNPLCLGLP VGPHQAPFDA SVQERIWLYN RRPPQFSRCV QYIHSFIHSL SFRLQDWSLD
FPSFLFPHIL YRQTRHSLSL HFTMKFTNIV LAASAATVAC AYPRGRDVIP TKQTADIKKR
GNGFTWVGVS ESGAEFGPGN VPGTLEKDYV WPKTSQIQIL RDAGMNIFRV PFLMERLVPS
SMTGSPDATY LAALKSTVKF ITDSGAYAVL DPHNYGRYNG NIITSTSDFK AFWKTVATQF
ASNEKVVFDT NNEYHDLDQT LVLNLNQAAI DAIRAAGATS QYIFVEGNSW SGAHSWTANN
DNLKALTDSE DKIVYEMHQY LDGDSSGTSE SCVSATIGKE RLESATAWLQ DNNKRGFIGE
FAGGVNSVCE SAVENMLSYM ADNSDVWMGA EWWAAGPWWG SYMYSLEPAD GPAYATYLPI
LEKYFVDGSS TPTKPSATST TTKAAPKTTT TTAAKTTTTA KAPTTTTAEV KVTTTANPNV
QVPTSSSSSS SSSTTTAAAK TTVVVAPIVP TTTTAPTTFV TATTTAKATA TTAATTTVKS
YEQVPTDSPS TGNIAKHYYQ CGGINWTGPT VCEAGTTCVV QNPYYHQCVS AL
//