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
//