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Database: UniProt
Entry: A0A093XQ67_9PEZI
LinkDB: A0A093XQ67_9PEZI
Original site: A0A093XQ67_9PEZI 
ID   A0A093XQ67_9PEZI        Unreviewed;       521 AA.
AC   A0A093XQ67;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
DE   Flags: Fragment;
GN   ORFNames=O988_07166 {ECO:0000313|EMBL:KFX92692.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX92692.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFX92692.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX92692.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 45 (cellulase K) family.
CC       {ECO:0000256|ARBA:ARBA00007793}.
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:KFX92692.1}.
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DR   EMBL; JPJR01001637; KFX92692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093XQ67; -.
DR   STRING; 1391699.A0A093XQ67; -.
DR   HOGENOM; CLU_523362_0_0_1; -.
DR   Proteomes; UP000029329; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000334; Glyco_hydro_45.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR   PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR   Pfam; PF02015; Glyco_hydro_45; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 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:UP000029329}.
FT   DOMAIN          301..521
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          67..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFX92692.1"
SQ   SEQUENCE   521 AA;  57183 MW;  BD743B631775B52B CRC64;
     PQYGTPSTGW GAQYGGISSR SQCDAFPEKL KAGCYWRFDW FQNADNPSVS FQSVACPLAI
     TNKSGCVRAD DKPTGDGSVP TVSGGAPPAT STGPGTTTPS SGTGNGGTVA KYAQCGGNGW
     TGGTGIPRGS GRSLKTPTAN NKPCPNIDFS CPTNTSLRES CIAPTTRCTS ESFSQISLRF
     SVEALYINSS IFTTRHTVID SQIDLPSSWV TVMCRATRFH ITISHKDIQS TRFATQYSKM
     VSSAIDDDGA EAHDELCEWM IDPCLSYFRE STSNVQKEIT FGDFYYPETH HLKLLVSGSE
     LSPKATRVSG TMNAFYLMIP SSDLPPSPEI PRLKASHLRI ISDPKWDDYM SEIPQKAIIA
     DGSTKFFKPA DDKKQILREV NMHMRIRRAR LQDLRIAKLH GIVVSDDGEM TIGLLLDLIP
     IPSTGDSLYS YRNSALAREY HERWKQQITD TVEQLHSHGL VWGDVHPGNI VIDTSFDAWV
     VDFGGGSIVE FVPRKMAGMK EGDWCGVGKV FNEWILENND N
//
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