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Database: UniProt
Entry: A0A1V6RWN1_9EURO
LinkDB: A0A1V6RWN1_9EURO
Original site: A0A1V6RWN1_9EURO 
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
//
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