ID A0A0A2JIT2_PENEN Unreviewed; 538 AA.
AC A0A0A2JIT2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN ORFNames=PEX2_028700 {ECO:0000313|EMBL:KGO55284.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO55284.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO55284.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO55284.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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; Evidence={ECO:0000256|ARBA:ARBA00001641};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000256|ARBA:ARBA00006044, ECO:0000256|RuleBase:RU361164}.
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:KGO55284.1}.
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DR EMBL; JQFZ01000200; KGO55284.1; -; Genomic_DNA.
DR RefSeq; XP_016597479.1; XM_016740145.1.
DR AlphaFoldDB; A0A0A2JIT2; -.
DR STRING; 27334.A0A0A2JIT2; -.
DR GeneID; 27675564; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OrthoDB; 3014058at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; Glycoside hydrolase, family 7, domain; 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; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 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; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361164};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361164};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361164};
KW Hydrolase {ECO:0000256|RuleBase:RU361164, ECO:0000313|EMBL:KGO55284.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361164};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..538
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001989698"
FT DOMAIN 502..538
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 464..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 56614 MW; EE7880AA3EB9B93C CRC64;
MASTLSFKIY KNALLLAAFL GAAQAQQVGT NTAEVHPSLT WQKCTAGGSC TSQSGKVVVD
ANWRWVHKTA GSTNCYTGNK WDTTICPDDV TCATNCALEG ADYSGTYGVT ASGSSLRLNF
VTQAYQKNIG SRLYLMADDS KYEMFHLLNQ EFTFDVDVSN LPCGLNGALY FVSMDEDGGM
ARYPANKAGA KYGTGYCDAQ CPRDLKFING QANVEGWEPS SNDVNAGTGN YGSCCAEMDI
WEANSISTAV TPHPCDDPAQ TRCSGDACGG TYSSDRYSGT CDPDGCDFNP YRMGNQSFYG
PSKIVDTKSP FTVVTQFITN DGTSAGTLSE IKRFYVQNGK VIPQSVSTIS AVTGNSITDS
FCSAQKTAFG DTDVFTQHGG LAGVGAGLAD GMVLVMSLWD DHAANMLWLD STYPTTASST
TPGAARGSCD ISSGEPTDVE ANHANAYVIY SNIKVGPLGS TFTSTGQGSG TTTTKATTTS
TTTTTSTTKA TTTTTTTGSS TTGAAQYAQC GGTNWTGATT CVSPYTCQKQ SEYYSQCL
//
